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 3, Problem 2Q
Summary Introduction

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The non-covalent bonds responsible for the interactionsindicated by the shaded regions in the given proteins.

Biochemistry: The Molecular Basis of Life, Chapter 3, Problem 2Q

Introduction:

Proteins are linear polymers of various amino acids. They are the fundamental macromolecules of a living cell, which are involved in various functions, such as transport, catalysis, movement, as well as structure. Examples of proteins are keratin, myosin, collagen, and fibroin. Protein molecules involve a number of bond, such as strong covalent bonds, ionic bonds, hydrogen bonds, as well as weak vanderWaal forces.

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All proteins have primary (1°), secondary (2°) and tertiary (3°) structure. In addition, some (but not all) proteins exhibit quaternary (4°) structure. Explain quaternary structure and why only some proteins exhibit that level of structure.
Hydrogen bonds and hydrochloric interactions play important roles in stabilizing and organizing biological macromolecules.  Describe how Hydrogen bonds and hydrochloric interactions affects the form and function of proteins.
At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.

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Biochemistry: The Molecular Basis of Life

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