清华本科生化考试 英文

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清华大学生物化学试卷2005_final_exam_A

清华大学生物化学试卷2005_final_exam_A
A.5
B.6
C.6.5
D.7.5
E.No ATP would form under these conditions.
Answer(s): D
3.Indicate which of the following events can occur during the processing of eukaryotic mRNA transcripts.
清华大学本科生考试试题专用纸(A)
考试课程Biochemistry II 2005年1月15日
说明:1.第1-40题为选择题,每题2分,答案可能是一个或多个,请将
正确答案填在适当的横线处;
2.第41-44题为问答题,每题的分数标在了题目后面,请将答案写
在答题纸上;
3.本卷满分为100。
1. Which compound links glycolysis, nucleotide synthesis, and glycogen synthesis?
Answer(s):D
8.Consider the mRNA sequence: (5’) AAUGCAGCUUUAGCA(3’). The sequence ofthe coding strand of DNA is:
A.(5’) ACGATTTCGACGTAA(3’)
B.(3’) TTACGTCGAAATCGT(5’)
E.The value ofG’ois also negative.
Answer(s): AD
13.Which of the following isnota physiological role of nucleotides?
A.allosteric regulators

生化本科题库题库Chapter 11 Test Bank

生化本科题库题库Chapter 11 Test Bank

Chapter 11 CarbohydratesMatching QuestionsUse the following to answer questions 1-10:Choose the correct answer from the list below. Not all of the answers will be used.a) Fehling’sb) enantiomersc) UDPd) glycogene) monosaccharidesf) celluloseg) lectinsh) Heparini) axialj) glycoproteinsk) epimersl) glycosyltransferases1 ____________ This class of compounds has the molecular formula of (CH2O)n.Ans: eSection: 11.12 ____________ These are stereoisomers that are mirror images of each other.Ans: bSection: 11.13 ____________ These monosaccharides differ at a single asymmetric carbon.Ans: kSection: 11.14 ____________ This is the most abundant organic molecule in the biosphere.Ans: fSection: 11.25 ____________ This is a test solution used to identify reducing and nonreducing sugars.Ans: aSection: 11.16 ____________ The storage form of glucose in animals.Ans: dSection: 11.27 ____________ This is an example of a glycosaminoglycan.Ans: hSection: 11.28 ____________ These are the enzymes that synthesize oligosaccharides.Ans: lSection: 11.29 ____________ Molecule to which most sugars are attached prior to transfer.Ans: cSection: 11.210 ____________ These proteins bind to specific carbohydrate structures.Ans: gSection: 11.3Fill in the Blank Questions11 A _______________ is a stereoisomer that is not a mirror image.Ans: diastereoisomer Section: 11.112 A _______________ is a five-membered ring formed from a monosaccharide.Ans: furanose Section: 11.113 A _______________ is formed when two monosaccharides are linked together via a glycosidicbond.Ans: disaccharide Section: 11.114 Plant starch is composed of amylose, a linear polymer of glucose, and a branched polymer ofglucose referred to as _______________.Ans: amylopectin Section: 11.215 Maltose is composed of two molecules of glucose linked together by ____________ glycosidicbond.Ans: α-1,4 Section: 11.216 _______________ is a galactose joined to a glucose by a β-1,4 glycosidic bond.Ans: Lactose Section: 11.217 In N-linked glycoproteins, the carbohydrate portion is attached to a(n)_____________ residue inthe protein.Ans: asparagine Section: 11.318 When the carbohydrate portion is attached to a serine or threonine residue in a glycoprotein, it isreferred to as a(n)_______________ glycoprotein.Ans: O-linked Section: 11.319 The influenza virus recognizes _______________ residues of glycoproteins present on cellsurface.Ans: sialic acid Section: 11.420 In C-type lectins, a _______________ acts as a bridge between the carbohydrate and the protein.Ans: calcium ion Section: 11.4Multiple Choice Questions21 Carbohydrates areA) polyhydroxy aldehydes.B) polyhydroxy ketones.C) polyhydroxy acids.D) polyhydroxy alcohols.E) a and b.Ans: E Section: Introduction22 The simplest carbohydrates areA) D- and L-glyceraldehyde.B) dihydroxyacetone and D- and L-glyceraldehyde.C) dihydroxyacetone and glycerate.D) All of the above.E) None of the above.Ans: B Section: 11.123 An aldehyde and alcohol can react to form aA) hemiaketal. D) All of the above.B) hemiketal. E) None of the above.C) hemiacetal.Ans: C Section: 11.124 Fructose can cyclize to (a)A) pyranose ring.B) furanose ring.C) both pyranose and furanose ring forms.D) All of the above.E) None of the above.Ans: C Section: 11.125 The nutritional storage form(s) of glucose in plants.A) glycogen B) amylose C) amylopectin D) b and c E) All of the aboveAns: D Section: 11.226 The enzyme that digests amylopectin.A) -amylase D) All of the above. B) amylose E) None of the above. C) celluloseAns: A Section: 11.227 To which amino acid residues in glycoproteins are the sugars commonly linked?A) tyrosine and asparagine D) serine and threonine B) serine, threonine, and asparagine E) a and d C) serine, tyrosine, and asparagine Ans: B Section: 11.328 Glycoproteins are normallyA) found on membranes.D) a and b.B) secreted as extracellular proteins. E) All of the above. C) found inside organelles.Ans: D Section: 11.329 At what sites in a cell are proteins glycosylated?A) ribosome D) b and c B) endoplasmic reticulum E) a, b, and c C) Golgi complexAns: D Section: 11.330 Which of the following is the anomer of β-D -glucopyranose?D)C)B)A)Ans: C Section: 11.231 Glycoforms refers toA) a single protein type that can have forms that vary in glycosylation. B) glycoproteins from the same gene family.C) a common core of sugars that can be found on many different proteins. D) all of the above. E) none of the above. Ans: A Section: 11.332 Selectins are proteins thatA) selectively bind proteins destined for lysozomes.B) aid in selection of proteins bound for the Golgi complex.C) bind immune-system cells as part of the inflammatory response.D) all of the above.E) none of the above.Ans: C Section: 11.433 What are lectins?A) proteins that bind the carbohydrates on glycoproteins and other macromoleculesB) proteins that promote cell-cell interactionC) proteins found in animals, plants, and microorganismsD) All of the above.E) None of the above.Ans: D Section: 11.4.34 How do some viruses gain entry into specific cells?A) by attaching to ion channelsB) by cleaving the glycosidic bonds and altering protein shapesC) by binding to glycoproteins on the cell surface that are unique to specific cellsD) All of the above.E) None of the above.Ans: C Section: 11.435 Inhibitors against this viral enzyme have potential as anti-influenza agents.A) calnexin D) All of the above.B) neuramidase E) None of the above.C) selectinAns: B Section: 11.4Short-Answer Questions36 List some of the reasons carbohydrates are considered important molecules.Ans: Carbohydrates serve several important functions as fuels, metabolic intermediates, and energy stores. They are the basis of most of the organic matter on our planet. Carbohydratesserve as the structural framework or building blocks for DNA, RNA, and polysaccharides.They are also linked to other molecules, such as proteins and lipids, and play importantroles in signaling and structure.Section: Introduction37 Draw the Fischer projection structures of all of the trioses.Ans: CH 2OH C CH 2OH O C C CH 2OHOH OH H C C 2OH O H HO H dihydroxyacetone D-glyceraldehyde L-glyceraldehyde Structures shown in Figure 11.1.Section: 11.1 and Figure 11.138 What is the difference between an enantiomer and a diastereoisomer?Ans: An enantiomer is a stereoisomer that is a perfect (nonsuperimposable or nonidentical)mirror image. A chiral molecule has one perfect mirror image. But for larger carbohydrates that have the same chemical formula and have multiple chiral centers, variations inasymmetric carbon structures mean that additional stereoisomers exist. The stereoisomers that are not mirror images of each other are called diastereoisomers.Section: 11.139 How is the D or L configuration determined?Ans: The D or L designation is determined by the asymmetric carbon farthest from the ketone oraldehyde group, and is related to the glyceraldehyde D and L structures.Section: 11.140 Draw the Haworth projections of the two pyranose forms of D -glucose.Ans:α-D -glycopyranose β-D -glucopyranose as shown in Figure 11.4 of the text.Section: 11.141 Draw the structure of lactose. Identify the monosaccharides involved and identify the type oflinkage in lactose? Ans:D-glucose (α anomer)Section: 11.242 Compare the structures of amylopectin and amylose.Ans: Both are homopolymers of glucose. Amylose consists of unbranched α-1,4 linkages of glucose. Amylopectin is a branched structure, and contains both α-1,4 linkages and α-1,6linkages, with the α-1,6 branches occurring about once every 30 glucose residues.Section: 11.243 What are the chemical and structural differences between cellulose and glycogen?Ans: Both are glucose homopolymers. Glycogen is a branched polymer and contains α-1,4 linkages with β-1,6 branchpoints about every 10 residues. Cellulose is a linear polymerthat contains β-1,4 linkages. Because of the β linkages, cellulose can form very longstraight chains which can form interchain hydrogen bonds to form fibrils.Section: 11.244 Describe some of the functions of glycosaminoglycans and proteoglycans.Ans: They function as lubricants, anticoagulents, and structural components; are important in pathways stimulating cell proliferation; and aid in mediating cell adhesion to extracellularmatrices.Section: 11.245 How does a genetic mutation account for some of the different human blood types?Ans: Blood type is determined by specific glycosyltransferases that add the end sugar to the glycoproteins found on red blood cells. Three different types of glycosyltransferase genescan be inherited, and each individual receives one from each parent. Two different formsresult in the A and B blood types. A mutation in a third type results in a truncated productthat is not active.Section: 11.246 What is the advantage of having different blood types within a species?Ans: Variations are protective because differences may be critical to protection against disease and infection. A microorganism that gains advantage over a host by mimicking and/orusing specific antigens, will not survive in host members that have differing antigens.Section: 11.247 Describe the mechanism by which N-linked sugars are synthesized and attached to proteins.Ans: The units are assembled in the ER attached to dolichol phosphate scaffold. Two N-acetylglucosamine residues and five mannose residues are added to form a commonprecursor, which is flipped into the ER lumen. Then specific enzymes adddolichol-phosphate-linked sugars, forming a 14-residue core. This is transferred to anasparagine residue on a protein, and the sugar core is processed by removal of three glucosemolecules. The addition and removal of other sugars in the Golgi complex further modifythe carbohydrate.Section: 11.3 and Figure 11.248 What are the two primary functions of the Golgi complex?Ans: The Golgi complex is 1) the site of carbohydrate addition and modification to glycoproteins, and 2) the major protein sorting center of the cell.Section: 11.349 What is the role of mannose 6-phosphate? What disease is caused by lack of this terminal sugar onglycoproteins?Ans: It acts as the marker that directs many lysozomal enzymes to their proper site. Without the modified mannose residue, the proteins are misdirected. For example, in I-cell disease,several enzymes are directed to blood and urine instead of the lysozomes. As a result,hydrolases required for glycosaminglycan and glycolipid degradation are missing, leadingto deformity and retardation.Section: 11.350 Why is it more difficult to determine the structure of the oligosaccharides, when compared toamino acid sequences?Ans: Amino acids are linked through peptide bonds and the side chains vary in size, charge, and chemical properties. In contrast, sugars can be branched, and can have α or β linkages,which makes determining the attachment difficult. Furthermore, many sugars have thesame or similar chemical formula, and similar chemical properties, making specificidentification and linkage difficult.Section: 11.3。

生化专业专升本英语作文模版

生化专业专升本英语作文模版

生化专业专升本英语作文模版Title: The Journey of Biochemical Specialization from Diploma to Bachelor's Degree.In the dynamic world of science and technology, biochemistry stands as a pivotal discipline, bridging the gap between the living world and the complexities of molecular interactions. My academic journey in biochemistry has been a transformative experience, taking me from the fundamentals of the subject at the diploma level to a deeper understanding and appreciation of its nuances at the bachelor's degree level.My initial interest in biochemistry stemmed from a curiosity about the inner workings of life. The intricate systems within cells, the dynamic processes of metabolism, and the intricate dance of enzymes and reactants fascinated me. At the diploma level, I gained a solid foundation in the basic principles of biochemistry, such as the structure and function of biomolecules, cellular metabolism, andgenetics. This foundation provided me with a solid starting point for my further studies.As I progressed to the bachelor's degree program, the scope and depth of the subject matter broadened significantly. I delved into areas such as proteomics, genomics, and bioinformatics, which gave me a more comprehensive understanding of the complex systems at play in biochemistry. The courses were more rigorous, and the concepts were more abstract, but the challenge was rewarding. I learned to think critically and analyze data, skills that are invaluable in the field of biochemistry.One of the most significant aspects of my bachelor's degree program was the opportunity to conduct research. Working in a laboratory environment gave me a taste of the real-world applications of biochemistry. I was able to apply the theoretical knowledge I had learned in the classroom to practical problems, gaining insights into the challenges and opportunities in the field. The research experience also taught me the importance of teamwork, communication, and perseverance.In addition to the academic aspects of my studies, I also gained a lot from the exposure to a diverse student body and a vibrant academic community. Interacting with peers from different backgrounds and perspectives broadened my horizons and enhanced my understanding of the subject. The collaborations and discussions in class and during group projects helped me develop a deeper understanding of biochemistry and its applications.Looking back on my journey from diploma to bachelor's degree in biochemistry, I am grateful for the opportunities and challenges that have shaped me as a student and afuture professional. The knowledge and skills I have gained have not only prepared me for a successful career in biochemistry but have also instilled in me a sense of curiosity and enthusiasm for lifelong learning.As I look ahead to the future, I am excited about the prospects of biochemistry and its role in addressing the challenges of our time, such as developing sustainable energy sources, improving health outcomes, andunderstanding the complexities of life at the molecular level. I am confident that my experience and expertise in biochemistry will enable me to contribute to these efforts and make a positive impact on society.In conclusion, my academic journey in biochemistry has been a rewarding and transformative experience. From the fundamentals of the subject at the diploma level to the advanced concepts and research opportunities at the bachelor's degree level, I have gained a deep understanding and appreciation of the beauty and complexity of biochemistry. I am excited about the future of this field and look forward to contributing to its progress and development.。

(完整word版)生物化学复试面试英语翻译

(完整word版)生物化学复试面试英语翻译

1.The repica of each strand of DNA has the base sequence of its complementarystrand,and from one strand,the other can be made。

This important characteristic of the molecule allows for the fidelity of DNA replication, transcription, and translation.DNA每条链的复制产物与其互补链相同,通过一条链,即可获得另一条链.DNA分子的这种重要特征确保了DNA分子的复制,转录,翻译的精确性。

2.Two major categories of enzymes are important tools in the isolation of DNA and the preparation of recombinant DNA: restriction endonucleases and DNA ligases. Restriction endonucleases recognize a specific, rather short, nucleotide sequence on a double—stranded DNA molecule, called a restriction site。

在DNA分离和重组DNA的获得过程中,有两类酶是重要的工具:限制性核酸内切酶以及DNA连接酶。

限制性核酸内切酶识别双链DNA分子上一个特定的、相当短的核酸序列,该序列被称作限制性位点。

3.Because its activity is easily detected by color reactions and its expression is inducible,β-galactosidase has become an important enzyme in DNA biotechnology。

大学英语生物学考试试题及答案

大学英语生物学考试试题及答案

大学英语生物学考试试题及答案考试试题:Section A: Multiple Choice Questions (共50题,每题1分,共50分)从A、B、C、D四个选项中,选出一个最佳答案,并将选项的字母代号填涂在答题卡相应的位置。

1. Which of the following is the study of relationships between organisms and their environments?A. PhysiologyB. GeneticsC. EcologyD. Evolution2. What is the primary role of ribosomes in a cell?A. Synthesis of lipidsB. Protein synthesisC. Cell divisionD. Energy production3. Which organelle is responsible for the production of ATP in eukaryotic cells?A. MitochondriaB. Endoplasmic reticulumC. NucleusD. Golgi apparatus4. Which of the following is responsible for the transportation of water and nutrients in plants?A. PhloemB. XylemC. StomataD. Chloroplasts5. What is the function of the respiratory system in humans?A. Regulation of body temperatureB. Production of hormonesC. Exchange of gasesD. Elimination of waste products...Section B: Short Answer Questions (共5题,每题10分,共50分)根据题目要求回答问题,并将答案写在答题卡上。

化学化工英语试题及答案

化学化工英语试题及答案

化学化工英语试题及答案一、选择题(每题2分,共20分)1. Which of the following is a chemical element?A. WaterB. OxygenC. HydrogenD. Carbon答案:B, C, D2. The chemical formula for table salt is:A. NaOHB. NaClC. HClD. NaHCO3答案:B3. What is the process called when a substance changes from a solid to a liquid?A. SublimationB. VaporizationC. MeltingD. Condensation答案:C4. In the periodic table, which group contains alkali metals?A. Group 1B. Group 2C. Group 17D. Group 18答案:A5. What is the name of the process where a substance decomposes into two or more substances due to heat?A. CombustionB. OxidationC. ReductionD. Decomposition答案:D6. Which of the following is a physical property of a substance?A. ColorB. TasteC. SolubilityD. Reactivity答案:A7. What is the term for a compound that releases hydrogen ions (H+) when dissolved in water?A. BaseB. AcidC. SaltD. Neutral答案:B8. The law of conservation of mass states that in a chemical reaction:A. Mass is lostB. Mass is gainedC. Mass remains constantD. Mass can be converted into energy答案:C9. Which of the following is a type of chemical bond?A. Ionic bondB. Covalent bondC. Hydrogen bondD. All of the above答案:D10. What is the name of the process where a substance absorbs energy and changes from a liquid to a gas?A. MeltingB. VaporizationC. SublimationD. Condensation答案:B二、填空题(每题2分,共20分)1. The symbol for the element iron is ________.答案:Fe2. The pH scale ranges from ________ to ________.答案:0 to 143. A compound that produces a basic solution when dissolvedin water is called a ________.答案:base4. The smallest particle of an element that retains its chemical properties is called a ________.答案:atom5. The process of separating a mixture into its individual components is known as ________.答案:separation6. The study of the composition, structure, and properties of matter is called ________.答案:chemistry7. The process of a substance changing from a gas to a liquid is called ________.答案:condensation8. A(n) ________ reaction is a type of chemical reactionwhere two or more substances combine to form a single product. 答案:synthesis9. The volume of a gas at constant temperature and pressureis directly proportional to the number of ________.答案:moles10. The process of converting a solid directly into a gas without passing through the liquid phase is known as ________. 答案:sublimation三、简答题(每题10分,共30分)1. Explain what is meant by the term "stoichiometry" in chemistry.答案:Stoichiometry is the calculation of the relative quantities of reactants and products in a chemical reaction.It is based on the law of conservation of mass and involvesthe use of balanced chemical equations and the molar massesof substances to determine the amounts of reactants needed to produce a certain amount of product or the amounts ofproducts formed from a given amount of reactant.2. Describe the difference between a physical change and a chemical change.答案:A physical change is a change in the state or form of a substance without altering its chemical composition. Examples include melting, freezing, and boiling. A chemical change, on the other hand, involves a change in the chemical composition of a substance, resulting in the formation of new substances. Examples include combustion and rusting.3. What are the three main types of chemical bonds, and givean example of each.答案:The three main types of chemical bonds are ionic bonds, covalent bonds, and metallic bonds. An ionic bond is formed when electrons are transferred from one atom to another, resulting in the formation of oppositely charged ions. An example is the bond between sodium (Na) and chloride (Cl) in table salt (NaCl). A covalent bond is formed when two atoms share electrons, as seen in water (H2O) where hydrogen atoms share electrons with oxygen. Metallic bonds occur in metals, where a "sea" of delocalized electrons is shared among positively charged metal ions, as in sodium metal。

清华大学生物化学练习题Test for Biochemistry II

清华大学生物化学练习题Test for Biochemistry II

31. In an attempt to determine whether a given RNA was catalytically active in the cleavage of a synthetic oligonucleotide, the following experimental results were obtained. When the RNA and the oligonucleotide were incubated together, cleavage of the oligonucleotide occurred. When either the RNA or the oligonucleotide was incubated alone, there was no cleavage. When the RNA was incubated with higher concentrations of the oligonucleotide, saturation kinetics of the Michaelis-Menten type were observed. Do these results demonstrate that the RNA has catalytic activity? Explain. (8 points)Answer: These results alone do not establish that the RNA has catalytic activity. A catalyst must be regenerated. It is entirely possible that the results observed could be accounted for by a stoichiometric, as opposed to a catalytic, interaction between RNA and the oligonucleotide. In which the RNA may “commit suicide”as the oligonucleotide is cleaved. In such an interaction, a portion of the RNA would also be cleaved itself as a part of the reaction. Four reaction products would accumulate, two resulting from the cleavage of RNA and two from the cleavage of the oligonucleotide. To show that this particular RNA was catalytic, it would be necessary to demonstrate that it turns over and is regenerated in the course of the reaction.32.Translation involves conversion of the language of nucleotides to that of proteins. In the chain of events leading from a nucleotide sequence on DNA to the production of protein by ribosomes, where precisely does the process of translation occur? Explain. (6 points)Answer: Translation involves conversion of the language of nucleotides to that of proteins. The agent of translation is the appropriate aminoacyl-tRNA synthetase, which must recognize a particular amino acid and link it to a tRNA containing an anticodon for that amino acid.33.Suppose that a bacterial mutant is found to replicate its DNA at a very low rate. Upon analysis, it is found to have entirely normal activity of DNA polymerases I and III, DNA gyrase, and DNA ligase. It also makes normal amounts and kinds of dnaA, dnaB, dnaC, and SSB proteins. The oriC region of its chromosome is found to be entirely normal with respect to nucleotide sequence. What defect might account for the abnormally low rate of DNA replication in this mutant? Explain. (6 points)Answer: A decrease in the activity of primase would account for the low rate of DNA replication. DNA replication requires the prior synthesis of RNA primers. Decreased rates of dNTP synthesis would also slow replication.。

生化--英文题

生化--英文题

生化历来都不画重点的,但留学生老是过不了,于是就有了这个重点资料,和我们考的差不多,但是英语的,求高人翻译啊Brief Exercises of BiochemistryChapter 1 The structure and function of proteinExplain the following terms1. peptide bond2. Amino acid residues3. Primary structure of protein4. isoelectric point5. Secondary structure of protein6. Tertiary structure of protein7. Domain8. Protein denaturation9. Quaternary structure of proteinAnswer the following questions briefly1. What is physiological significance of hemoglobin oxygen dissociation curve as S-shaped?2. Please describe physiological functions of proteins.Discuss the following questions (Essay questions)1. Explain the relationship between the primary and spatial structure and the function of protein.Chapter 2 The structure and function of nucleic acidsExplain the following terms1. primary structure of nucleic acids2. DNA denaturation3. Tm4. DNA renaturation5. nucleic acid hybridizationAnswer the following questions briefly1. What is the structural characteristics of an eukaryocyte mature mRNA?2. What is the biological significance of Tm?Discuss the following questions (Essay questions)1. Please compare the two types of nucleic acids (DNA and RNA) in the chemical composition, molecular structure, cell distribution and biological functions.2. Please describe the structural characteristics of the B-DNA.3. Describe the molecular composition, structural features and functions of tRNA.Chapter 3 EnzymeExplain the following terms1. enzyme2. enzyme active center3. enzyme competitive inhibition4. Km5. isoenzyme6. zymogen activationAnswer the following questions briefly1. Explains with examples the competitive inhibition characteristic and the practical significance.2. What is the relationship between the enzyme cofactor and vitamine?3. What is the physiological significance of zymogen?4. What is isoenzyme? What is clinical significance of isoenzyme?5. How many kinds of essential group of enzyme are there? What is the role of each?Chapter 4 Metabolism of carbohydrateExplain the following terms1. glycolysis2. glycolytic pathway3. tricarboxylic acid cycle4. gluconeogenesis5. blood sugarAnswer the following questions briefly1. Describe briefly source and fate of blood sugar2. Describe briefly the physiological significance of gluconeogenesis3. Describe briefly the physiological significance of glycolysis4. Describe briefly the outline of TCA cycle5. Describe briefly the physiological significance of TCA cycle6. Describe briefly the physiological significance of pentose phosphate pathway7. Outline the reasons for the formation of lactic acid cycle and the physiological significance.8. Overview the important role of B vitamins in glucose metabolism.9. Why 6-phosphate glucose dehydrogenase activity will increase after uptake high-carbohydrate diet?Discuss the following questions (Essay questions)1. Explain how is lactate converted into glucose? (Write down the main reactions and key enzymes)2. Explain how is lactate converted into CO2, H2O and releases ATP? (Write down the main reactions and key enzymes)3. Overview the regulation molecular mechanism of adrenaline on the blood sugar level.4. Please explain why a slimmer has to reduce the intake of carbohydrates from the point of view of nutrients metabolism. (Write down the related pathways, cellular localization, main reactions and key enzyme)Chapter 5 Metabolism of lipidsExplain the following terms1. fat mobilization2. ketone body3. plasma lipoprotein4. apolipoprotein5. essential fatty acid6. blood lipidsAnswer the following questions briefly1. What is the function of bile acid at lipids digestion?2. What is the physiological significance of ketone body generation?3. What are materials of fatty acid synthesis?4. What is the physiological significance of cholesterol?5. What are the functions of apolipoprotein?Discuss the following questions (Essay questions)1. Describe the sources, chemical composition characteristics and main physiological functions of plasma lipoprotein.2. Explain how is the stearic acid converted into CO2, H2O and releases ATP?3. Please describe the oxidation catabolism process of glycerol generated from fat mobilization4. Explain how is the glycerol converted into glycogen?5. Describe the source and fate of acetyl-CoA?Chapter 6 Biological oxidationExplain the following terms1. biological oxidation2. respiratory chain3. oxidative phosphorylation4. substrate level phosphorylationDiscuss the following questions (Essay questions)1. Write down the sequence of two respiratory chainChapter 7 Metabolism of amino-acidExplain the following terms1. essential amino acid2. deamination of amino acid3. transamination of amino acid4. one carbon unit5. hyperammonemiaAnswer the following questions briefly1. What is the physiological significance of one carbon units?2. What is meaning of PAPS, GABA, SAM and FH4 each?3. Write down the deamination of amino acids in vivo.4. Outline the source and fate of blood ammonia.Discuss the following questions (Essay questions)1. How does a glutamate be oxidized to supply energy? What is the final product?2. What are functions of vitamins B in the metabolism of amino acids?3. Use the alanine as an example, try to explain the gluconeogenesis process of glucogenic amino acids.Chapter 8 Metabolism of nucleotideExplain the following terms1. de novo synthesis pathway of purine nucleotide2. nucleotide antimetaboliteAnswer the following questions briefly1. Outline the biological function of nucleotide.2. Outline the physiological significance of salvage synthesis of purine nucleotide.Discuss the following questions (Essay questions)1. Use the 6-mercaptopurine as an example, please explain the mechanism of antimetabolite.Chapter 10 Biosynthesis of DNAExplain the following terms1. semi-conservative replication2. reverse transcription3. replication4. excision repairing5. frame-shift mutationAnswer the following questions briefly1. Outline the classification and function of prokaryote DNA polymerase.2. Outline the classification and function of eukaryote DNA polymerase.3. Outline the factors causing DNA damage.4. Outline the repairing of DNA damage.5. Outline the central dogma.Discuss the following questions (Essay questions)1. Describe the materials involved in prokaryote DNA replication and their functions in that process.2. Describe the biological significance of mutation.Chapter 11 Biosynthesis of RNAExplain the following terms1. transcription2. posttranscriptional process3. hnRNA4. promoter5. ribozyme6. structure geneAnswer the following questions briefly1. Outline the eukaryote posttranscriptional process.2. Outline the products of three kinds of eukaryote RNA polymerases.Discuss the following questions (Essay questions)1. Describe the similarity and dissimilarity of replication and transcription.Chapter 12 Biosynthesis of proteinExplain the following terms1. translate2. polyribosomes3. genetic code4. degeneracy of codonAnswer the following questions briefly1. Describe briefly the RNAs involved in the protein synthesis and their functions in that process.2. Outline the main features of the genetic code.3. Describe briefly the dissimilarity of translation initiation complex formation of prokaryotes and eukaryotes.Discuss the following questions (Essay questions)1. Describe the materials involved in protein biosynthesis and their functions in that process.3. Please comparing the process of translation of prokaryotes and eukaryotes.Chapter 13 The regulation of gene expressionExplain the following terms1. gene expression2. cis-acting element3. trans-acting factor4. operon5. general transcription factor6. enhancerAnswer the following questions briefly1. What is biological significance of regulation of gene expression?2. Outline the function of each component of operon.3. What characteristics does eukaryotic genome structure have?Discuss the following questions (Essay questions)1. Explain the regulation mechanism of lactose operon.Chapter 14 Gene recombination and gene engineeringExplain the following terms1. restriction endonuclease2. genomic DNA3. vector4. cDNA. library5. genetic engineering6. DNA cloning7. homologous recombinationAnswer the following questions briefly1. What are the main selection criteria of gene vector?2. What is the significance of restriction endonuclease of bacteria themselves?3. At present, How many ways to get target genes?4. Outline the basic process of DNA cloning.Discuss the following questions (Essay questions)1. Why plasmid can be used as the vector of genetic engineering?2. Explain how to connect the foreign gene and the vector.3. What is α-complementary? Explain how to screening recombinant by it using an example.Chapter 15 Cellular signal transductionExplain the following terms1. signal transduction2. receptor3. ligand4. signal transduction pathway5. protein kinase6. second messenger7. G proteinAnswer the following questions briefly1. Describe briefly which protein kinases are regulated by intracellular second messenger.2. Outline the classification of receptor and its chemical signals.3. Describe briefly the basic mode of G protein-coupled receptor (seven transmembrane receptor)-mediated signal transduction.4. Describe briefly the signal transduction pathway of intracellular receptor of steroid hormone.Discuss the following questions (Essay questions)1. How does intracellular receptor play its function?2. Explain the process of the glycogen metabolism regulated by glucagon.3. Use fat mobilization as an example, explain the process of cAMP-protein kinase pathway. Chapter 16 Blood biochemistryExplain the following terms1. 2, 3-BPG shuntAnswer the following questions briefly1. Outline the function of plasma protein.Chapter 17 Liver biochemistrExplain the following terms1 biotransformation 2. primary bile acid 3. secondary bile acid4. bile pigment5. jaundiceAnswer the following questions briefly1. Describe briefly the physiological significance of biotransformation.2. Outline the main physiological functions of bile acids.3. Describe briefly production and blood transportation of bilirubin.Discuss the following questions (Essay questions)1. Describe the influence factor of biotransformation.2. Explain the dissimilarity of unconjugated and conjugated bilirubin.Chapter 18VitaminsExplain the following terms1. vitamin2. lipid-soluble vitamin3. water-soluble vitaminAnswer the following questions briefly1. Outline the biochemical function of vitamin E.2. Describe briefly the biochemical function of vitamin D and its deficiency disease.Discuss the following questions (Essay questions)1. Explain the relationship between the water-soluble vitamin and the coenzyme. Chapter 20 Oncogenes, tumor suppressor genes and growth factorExplain the following terms1. oncogene2. proto-oncogene3. tumor suppressor geneAnswer the following questions briefly1. Describe characteristics of proto-oncogene.2. Describe briefly wild-type p53 tumor suppressor gene mechanism.Chapter 21 The Principle and Application of Common Used Techniques in Molecular Biology Explain the following terms1. probe2. PCR3. Gene diagnosis4. gene therapyDiscuss the following questions (Essay questions)1. Describe the definition, type and application of the blotting technique.2. Describe the PCR reaction principle and the basic steps.。

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清华大学本科生考试试题专用纸考试课程Biochemistry II 2001 年 6 月 11 日说明:1. 请选择正确答案,填在适当的横线处(1-30题)或写在答题纸上(31 -33题);2. 答案可能是一个或多个;3. 每题的分数在标在了题目后面;4. 本卷满分为100.G` of the∆1. If the reaction A B is –12 kJ/mol, which of the following statements are correct? (Note the prime symbol means that a thermodynamic parameter is measured at pH.7.0) (2 points)A. The reaction will proceed spontaneously from left to right at the given conditions.B. The reaction will proceed spontaneously from right to left at stan dard conditions.C. The equilibrium constant favors the formation of B over the format ion of A.D. The equilibrium constant could be calculated if the initial concen trations of A and B were known.E. The G`o is also negative.∆value ofAnswer(s): A, D2. Which of the following statements about ATP and its roles in cells are true? (2 points)A. The ATP molecule is kinetically unstable and is thus consumed with in about one minute following its formation in cells.B. ATP provides free energy to a thermodynamically unfavorable reacti ons by group transfer, always donating a Pi to form a covalent interm ediate.C. ATP can be regenerated by coupling with a reaction that releases m ore free energy than does ATP hydrolysis.D. A transmembrane proton-motive force can drive ATP synthesis.E. The active form of ATP is usually in a complex with Mg2+.Answer(s): C, D, E3. A common moiety for NADP, NAD, FMN, FAD, and coenzyme A is: (2 poi nts)A. A pyrimidine ring;B. A three ring structure;C. An ADP;D. A pyranose ring;E. A triphosphate group.Answer(s): C4. If the C-1 carbon of glucose were labeled with 14C, which of the c arbon atoms in pyruvate would be labeled after glycolysis? (2 points)A. The carboxylate carbon;B. The carbonyl carbon;C. The methyl carbon.Answer(s): C第页/共页5. Which of the following are metabolic products of pyruvate in highe r organisms? (2 points)A. GlycerolB. Lactic acidC. AcetoneD. Acetyl-CoAE. EthanolAnswer(s): B, D6. Indicate whether each of the following statements about the pentose phosphate pathway is true (T) or false (F). (5 points)A. It generates NADH for reductive biosyntheses. FB. The reactions occur in the cytosol. TC. Transketolase and transaldolase link this pathway to gluconeogenes is. FD. It is more active in muscle cells than in fat-storage cells. FE. It interconverts trioses, tetroses, pentoses, hexoses, and heptose s. T7. Which of the following statements are correct? The citric acid cyc le (2 points)A. does not exist as such in plants and bacteria, because its functio ns are performed by the glyoxylate cycle.B. oxidizes acetyl CoA derived from fatty acid degradation.C. produces most of the CO2 in anaerobic organisms.D. provides succinyl CoA for the synthesis of carbohydrates.E. provides precursors for the synthesis of glutamic and aspartic aci ds.Answer(s): B, E8. Match the cofactors of the pyruvate dehydrogenase complex with the ir corresponding enzyme components and with their roles in the enzymatic steps that are listed. (5 points)A. Coenzyme A: 3,7B. NAD+: 2, 9C. Thiamine pyrophosphate (TPP): 1, 5D. FAD: 2, 6E. Lipoamide: 3, 4,8(1). Pyruvate dehydrogenase component(2). Dihydrolipoyl dehydrogenase(3). Dihydrolipoyl transacetylase(4). Oxidizes the hydroxylethyl group(5). Decarboxylates pyruvate(6). Oxidizes dihydrolipoamide(7). Accepts the acetyl group from acetyllipoamide(8). Provides a long, flexible arm that coveys intermediates to diffe rent enzyme component.(9). Oxidizes FADH2.9. Matching the role in fatty acid oxidation and/or mobilization to t he appropriate component listed below. (5 points)A. Bile salt: 2B. Serum albumin:5C. ApoC-II:4D. Apolipoprotein:3E. Carnitine:1(1). Acts as a “carrier” of fatty acids across the inner mitochondr ial membrane.(2). Acts as a biological detergent, disrupting fat globules into sma ll mixed micelles.(3). Binds and transports triacylglycerols, phospholipids, and choles terol between organs.(4). Activates lipoprotein lipase, which cleaves triacylglycerols int o their components.(5). Binds some fatty acids molibized from adipocytes and transports them in the blood to heart and skeletal muscle.第页/共页10. Which of the following answers complete the sentence correctly? S urplus dietary amino acids may be converted into (2 points)A. proteins.B. Fats.C. ketone bodies.D. glucose.E. a variety of biomolecules for which they are precursors.Answer(s): A, B, C, D,E11. Which of the following compounds serves as an acceptor for the am ino groups of many amino acids during metabolism? (2 points)A. GlutamineB. Asparagine.C. -ketoglutarate.D. OxaloacetateE. GlutamateAnswer(s):C12. Match the functions for the coenzymes that are involved in amino acid metabolism. (4 points)A. Pyridoxal phosphate: (3)B. Coenzyme B12: (2)C. Tetrahydrobiopterin: (1)D. NAD+: (1)E. Biotin (4)(1). Carries electrons(2). Provides free radicals(3). Carries amino groups(4). Carries CO2.13. Which of the following experimental observations would not suppor t the chemiosmotic model of oxidative phosphorylation? (3 points) A. If mitochondrial membranes are ruptured, oxidative phosphorylation cannot occur.B. Raising the pH of the fluid in the intermembrane space results in ATP synthesis in the matrix.C. Transfer of electrons through the respiratory chain results in for mation of a proton gradient across the inner mitochondrial membrane.D. The orientation of the enzyme complexes of the electron transfer c hain results in a unidirectional flow of H+.E. Radioactively labeled inorganic phosphate is incorporated into cyt osolic ATP only in the presence of an H+ gradient across the inner mi tochondrial membrane.Answer(s): B14. Some photosynthetic prokaryotes use H2S, hydrogen sulfide, instead of water as their photosynthetic hydrogen donor. How does this chan ge the ultimate products of photosynthesis? (2 points)A. Carbohydrate (CH2O) is not produced.B. H2O is not produced.C. Oxygen is not produced.D. ATP is not produced.E. The products do not change.Answer(s): C15. Which of the following are constituents of chlorophylls? (2 point s)A. Substituted tetrapyrrole.B. Plastoquinone.C. Mg2+.D. Fe2+.E. Phytol.F. Iron porphyrin.Answer(s): A, C, E第页/共页16. The observation that the incubation of photosynthetic algae with 14CO2 in the light for a very brief time (5s) led to the formation of 14C-labeled 3-phosphoglycerate suggested that the 14CO2 was condensi ng with some two-carbon acceptor. That acceptor was in fact which of the following? (2 points)A. AcetateB. Acetyl CoAC. Acetyl phosphateD. AcetaldehdydeE. Glycerol phosphateF. None of the aboveAnswer(s): F17. Which of the following are common features of the syntheses of me valonate (an intermediate of cholesterol biosynthesis) and ketone bod ies? (2 points)A. Both involve 3-hydroxyl-3-methylglutaryl CoA (HMG-CoA).B. Both require NADPH.C. Both require the HMG-CoA cleavage enzyme.D. Both occur in the mitochondria.E. Both occur in liver cells.Answer(s): A18. S-adenosylmethionine is involved directly in which of the followi ng reactions. (3 points)A. Methyl transfer to phosphatidyl ethanolamine.B. Synthesis of glycine from serine.C. Synthesis of polyamines.D. Conversion of homocysteine to methionine.E. Generation of the 5` cap of the eukaryotic mRNAs.Answer(s): A, C, E19.Which of the following does not provide a carbon skeleton for thesynthesis of amino acids? (2 points)A. succinate.-ketoglutarate B.C. Pyruvate.D. Oxaloacetate.E. Ribose-5-phosphate.Answer(s): A20. Which of the following compounds directly provide atoms to form t he purine ring? (3 points)A. Aspartate.B. Carbamoyl phosphate.C. Glutamine.D. Glycine.E. CO2.F. N5,N10-methylenetetrahydrofolate.G. N10-formyltetrahydrofolate.H. NH4+.Answer(s): A, C, D, E, G21. Which of the following statements about ribonucleotide reductase are true? (2 points)A. It converts ribonucleoside diphosphates into 2`-deoxyribonucleosid e diphosphates in humans.B. It contains coenzyme B12, which generates free radicals needed for the catalysis.C. It accepts electrons directly from FADH2.D. It receives electrons directly from either thioredoxin or glutared oxin.E. It contains two kinds of allosteric regulatory sites: one for cont rolling the overall activity and the other for controlling the substr ate specificity.Answer(s): A, D, E22. Biosynthetic pathways that require NADPH include which of the fol lowing? (2 points)A. Gluconeogenesis.B. Fatty acid biosynthesis.C. Ketone body formation.D. Cholesterol biosynthesis.E. Tyrosine biosynthesis.Answer(s): B,D,E23. Homologous recombination in E. coli is likely to require which of the following? (3 points)A. DnaB protein.B. RecA protein.C. RecBCD complex.D. ATP.E. NAD+.F. Single-strand DNA binding protein.G. DNA-dependent RNA polymerase.H. DNA polymerase I.I. DNA ligase.J. dATP.Answer(s): B, C, D, E, F, H, I, J24. Which of the following statements about E. coli promoters are cor rect? (2 points)A. They may exhibit different transcription efficiencies.B. For most genes they include variants of consensus sequences.C. They specify the start sites for transcription on the DNA template.D. They have identical and defining sequences.E. They are activated when C or G residues are substituted into their–10 regions by mutation.F. Those that have sequences that correspond closely to the consensus sequences and are separated by 17 base pairs are very efficient. Answer(s): A, B, C, F25. The AAUAAA sequence on a RNA molecule marks (2 points)A. The site where ribosomes bind to initiate polypeptide synthesis.B. The site where transcription stops.C. The site near which the primary transcript is cleaved and a poly (A) sequence is added.D. The site where the release factor will bind to end polypeptide syn thesis.E. The site where polyribonucleotide phosphorylase will add a stretch of random sequences.Answer(s): C70 subunit of the 26. The E. coli RNA polymerase: (2 points)A. acts as the catalytic site for polymerization.B. Recognize promoters.C. Has a proofreading function.D. Increases the processivity of the enzyme.E. Recognizes termination signals.Answer(s): B27. The discontinuity of eukaryotic genes were first revealed by: (2 points)A. Using footprinting techniques.B. DNA sequence comparison.C. RNA sequence analysis.D. Electron microscopic analysis of RNA-DNA hybrid molecules.E. Plant genetic studies.Answer(s): D第页/共页28. Which of the following mRNA codons can be recognized by the tRNA anticodon ICG. (2 points)A. UGC.B. CGA.C. UGA.D. CGU.E. CGC.Answer(s): B, D, E29. A new compound, vivekine, was recently discovered by a clever und ergraduate student. It was isolated from bacteria found in deep sea-d welling organisms. Vivekine inhibits protein synthesis in eukaryotes: Protein synthesis can initiate, but only dipeptides are formed and t hese remain bound to the ribosome. This toxin affects eukaryotic prot ein synthesis by blocking the: (2 points)A. binding of formylmethionyl-tRNA to ribosomes.B. activity of elongation factors.C. activation of amino acids.D. recognition of stop signals.E. formation of peptide bonds.Answer(s): B30. Indicate whether each of the following statements about prokaryot ic translation is true (T) or false (F). (7 points)A. An aminoacyl-tRNA synthetase catalyzes formation of an ester bond. ( T )B. An mRNA molecule cannot be used to direct protein synthesis until it has been completely transcribed. ( F )C. The positioning of fMet-tRNA on the A site defines the reading fra me. ( F )D. Incoming aminoacyl-tRNA are first bound to the A site. ( T )E. Formation of the 70S initiation complex requires an input of energ y. ( T )F. The carboxyl group of the amino acid on the aminoacyl-tRNA is transferred to the amino group of a peptidyl-tRNA.( F )G. Release factors cause the peptidyl transferase activity of the rib osome to use H2O as a substrate. ( T )第页/共页31. In an attempt to determine whether a given RNA was catalytically active in the cleavage of a synthetic oligonucleotide, the following experimental results were obtained. When the RNA and the oligonucleot ide were incubated together, cleavage of the oligonucleotide occurred. When either the RNA or the oligonucleotide was incubated alone, ther e was no cleavage. When the RNA was incubated with higher concentrati ons of the oligonucleotide, saturation kinetics of the Michaelis-Ment en type were observed. Do these results demonstrate that the RNA has catalytic activity? Explain. (8 points)Answer: These results alone do not establish that the RNA has catal ytic activity. A catalyst must be regenerated. It is entirely possibl e that the results observed could be accounted for by a stoichiometri c, as opposed to a catalytic, interaction between RNA and the oligonu cleotide. In which the RNA may “commit suicide” as the oligonucleot ide is cleaved. In such an interaction, a portion of the RNA would al so be cleaved itself as a part of the reaction. Four reaction product s would accumulate, two resulting from the cleavage of RNA and two fr om the cleavage of the oligonucleotide. To show that this particular RNA was catalytic, it would be necessary to demonstrate that it turns over and is regenerated in the course of the reaction.32.Translation involves conversion of the language of nucleotides to that of proteins. In the chain of events leading from a nucleotide se quence on DNA to the production of protein by ribosomes, where precis ely does the process of translation occur? Explain. (6 points)Answer: Translation involves conversion of the language of nucleotid es to that of proteins. The agent of translation is the appropriate a minoacyl-tRNA synthetase, which must recognize a particular amino aci d and link it to a tRNA containing an anticodon for that amino acid.33.Suppose that a bacterial mutant is found to replicate its DNA at a very low rate. Upon analysis, it is found to have entirely normal ac tivity of DNA polymerases I and III, DNA gyrase, and DNA ligase. It a lso makes normal amounts and kinds of dnaA, dnaB, dnaC, and SSB proteins. The oriC region of its chromosome is found to be entirely normal with respect to nucleotide sequence. What defect might account for t he abnormally low rate of DNA replication in this mutant? Explain. (6 points)Answer: A decrease in the activity of primase would account for the low rate of DNA replication. DNA replication requires the prior synth esis of RNA primers. Decreased rates of dNTP synthesis would also slo w replication.第页/共页(中国生物论坛 copyright reserved)。

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