生化第五章（Biochemical fifth chapters）.docVIP

生化第五章（Biochemical fifth chapters） The fifth chapter is the three-dimensional structure of proteins exercises 1. (1) calculates the axial length of an alpha helix with 78 amino acids. (2) how long is the alpha helix of this polypeptide fully extended? [11.7nm; 28.08nm] Solution: (1) each residue in the alpha helix rotates about 100 degrees along the axis and rises 0.15Nm along the axis, so the axis of the alpha helix is: 78 x 0.15nm=11.7nm (2) alpha helices each spiral accounted for 3.6 amino acid residues, the alpha helix number is: 78 / 3.6 ring; alpha helix diameter is about 0.5nm and the length of each circle 0.5 PI nm. The alpha helix length fully extended approximately: 0.5 pi * (78 / 3.6) = 34.01nm. 2. a polypeptide chain of a protein, except for some sections, is the alpha helix, and the other sections are in the form of beta folded conformation. The relative molecular mass of protein is 240000, the length of the polypeptide chain family name is 5.06 * 10-5cm. The alpha helix accounted for the percentage of the polypeptide chain. (assuming that the length of a disability per amino acid in a beta fold conformation is 0.35nm) [59%] Solution: general average molecular weight of 120Da amino acids, molecular weight of the protein is 240000Da, so the number of amino acid residues was 240000 120=2000. There are X amino acid residues with an alpha helix structure: X, 0.15+ (2000-X) * 0.35=5.06 * 10-5 * 107=506nm The length of the alpha helix is 970 x 0.15=145.5, so the percentage of the alpha helix in the protein molecule is X=970: 145.5/536 * 100%=29% 3. although in vacuum hydrogen bond energy is about 20kj/mol, but in the folding of the protein in its protein masthead enthalpic contribution is much smaller (5kj/mol). Try to explain the difference. Most of hydrogen bonds in the protein in the body stretch and acceptance body with water to form hydrogen bonds. The reason for the small contribution of hydrogen bond energy to stable enthalpy during depreciation. ] 4. p