课程名称︰生物化学上 课程性质︰农化生技系必修 课程教师︰张世宗 开课学院：生农学院 开课系所︰ 考试日期（年月日）︰99/10/26 考试时限（分钟）：110分钟 是否需发放奖励金：是 1.Please briefly describe the Miller-Urey experiment and what compounds can be produced? 2.What do "homologs", "paralogs", and "orthologs" stand for? 3 In ice how many hydrogen bonds can each water molecule form with other water molecules? What is the approximate bond length between the hydrogen atom of one water molecule and the oxygen atom of a second water molecule in ice? 4.Please address the essential factors for forming strong hydrogen bonds. 5.The entropy of binding of a substrate to an enzyme is frequently posivive. Why? 6.Please address the van der Waals radii. 7.Please list four types of noncovalent interactions among biomolecules in aqueous solvent and why noncovalent interactions in biomolecules are so important for biochemical reaction? 8.The buffering region of a weak acid/base buffer is about how much pH unit? 9.Please answer the following questions about amino acids. For getting the full credits, please write the answer in full names, three letter abbreviations and one-letter codes. (a)The amino acid does not have a chiral alpha-carbon atom. (b)The amino acids contain a sulfur atom. (c)The amino acids contain a hydroxyl groups. (-OH) (d)The amino acids that have two chiral carbons. (e)The amino acid showing in a square box on the right. (f)By using the RS system for describing amino acid, which L-amino acid has the (g)The amino acid contains aromatic R group. 10.Draw the structural formulate of L-histidine and L-proline. 11.Arrange glutamate, asparatate, histidine, arginine and lysine in order according to their pKR values.(from small to large) 12.Please calculate the approximate pI value of Leu-Glu-Ala-Arg-Val-His-Ala (pK2 of leu=9.6, pKR of Glu=4.25, pKR of Arg=12.48, pKR of His=6.0, pK1 of Ala=2.34) 13.Definition of one unit of enzyme activity. 14.Descibe the biochemical term "specific activity" 15.Briefly describe two dimensional gel electrophoresis. 16.Describe the working condition to fully hydrolyze a polypeptide to its constisuent amino acids. 17.Please describe the procedure of Edman degradation for determinating the res 18.Schiff base. 19.Which of the following compound can interact with the amino groups of amino 20.Which of the following compound can interact with the -SH group of cysteine? 21.What kind of peptide fragments will be produced by incubating A-L-K-M-H-A-R-D-M-L-K with cyanogens bromide(CNBr)? 22.What kind of peptide fragments will be produced by incubating A-L-K-M-H-A-R-D-M-L-K with trypsin? 23.What the term m/z stand for in mass spectrometry analysis? 24.Draw two planar peptide groups with atoms, and indicate the dihedral angles Φ andΨ. 25.Why peptide bond is rigid and coplanar? 26.How many amino acid residues consist of one turn of alpha-helix? And how much is the rise along the helical axis for each residues? 27.Describe all C=O groups point which terminus, and R groups point toward which direction in alpha-helix? 28.What is the major weak interaction for stabilizing the beta conformation of polypeptide chains? 29.How many residues are involved in a beta-turn? In order to form a hydrogen bond between residue 1 and 4, the type II beta turn usually has which amino acid at position 3? 30.What is the repeated amino acid triplet for composing of collagen? 31.Why vitamin C (ascorbic acid) deficiency may lead to scurvy? 32.Fibroin consists of layers of anti-paralled beta sheets rich in what kinds of amino acids? 33.Explain (a)Tm (b)Denaturation (c)Motif (d)Domain 34.Provide five methods for denaturing proteins. 35.Describe the denaturation and renaturation experiment of ribonuclease A demonstrated by Anfinsen in 1950s, and what are the major conclusions addressed by Anfinsen based on the experimental results? 36.Please describe the hydrophobic collapse and molten globule protein folding model. 37.What are the functions of molecular chaperones and chaperonins? 38.Please describe one kind of disease caused by protein misfolding or defects in protein folding. --

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