Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 3.2, Problem 1R
Summary Introduction
To review:
The occurrence of change in the tertiary or the secondary structure of protein on replacement of one lysine residue by aspartic acid and the mechanism of this replacement.
Given:
One lysine residue is replaced by an aspartic acid residue in the protein.
Introduction:
The alteration in the primary structure takes place on replacement of one amino acid with another. The aspartic acid has negative change due to the presence of −COO− (carboxyl group) and the lysine has positive change due to presence of −NH3 (amino group). Amino acids that were initially bonded to aspartic acid get detached and new amino acids bind to the lysine residues on the replacement of aspartic acid with lysine.
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Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.
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- Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?arrow_forwardOur growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.arrow_forwardThe addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.arrow_forward
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