課程名稱︰生物化學上
課程性質︰農化生技系必修
課程教師︰張世宗
開課學院：生農學院
開課系所︰
考試日期（年月日）︰99/10/26
考試時限（分鐘）：110分鐘
是否需發放獎勵金：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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