Biochemistry: The Molecular Basis of Life
Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 5, Problem 55TQ
Summary Introduction

To review:

The way in which protein molecules incorporate large amounts of immobilized water and make it a part of their structure.

Introduction:

Water playsan important role in governing the structure and stability of proteins. Water molecules participate in hydrogen bonding and electrostatic interactions with the side chains of amino acids present on the surface of the protein. In the structure of a protein, there are hydrophobic side chains that are excluded from the water. These increase the entropy of water molecules.

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Question 4. Imagine the main chain of a protein bends back on itself so that two amino acid residues R1 and R2 come close to each other. In the table below are four possibilities for what R1 and R2 might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ cysteine tyrosine threonine arginine R₂ cysteine phenylalanine glutamine aspartate specific interaction? OO yes O yes O no no OO O yes no yes no name of specific interaction 0 П 0 0
Question 25 Calculate the net charges of the following peptides at pH 7.4. Indicate which amino acids bear chuarged side chans a) NH2-Asp-Leu-Phe-Ala-Lys-Pro-Glu-Gly-COOH b) NH2-GIn-Glu-Lys-Tyr-Trp-Arg-Ala-Leu-COOH DELL
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH

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Biochemistry: The Molecular Basis of Life

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