Chapter 3, Problem 21P

(a)

Summary Introduction

To determine: The amino acid residues that are invariant in the given sequence.

Introduction:

Protein folding is a process, by which a protein molecule acquires biologically functional $\text{3-D}$ (three-dimensional) conformation from its random coiled structure. After translation, proteins have an unfolded linear chain of amino acids. This protein or polypeptide begins to fold into $\text{3-D}$ structure as it is synthesized within the ribosome. Chaperones are molecules that assist protein folding.

(b)

Summary Introduction

To determine: The positions at which the amino acids are limited to those with positively charged side chains and which amino acid predominates at each position

Introduction:

Protein folding is a process, by which a protein molecule acquires biologically functional $\text{3-D}$ (three-dimensional) conformation from its random coiled structure. After translation, proteins have an unfolded linear chain of amino acids. This protein or polypeptide begins to fold into $\text{3-D}$ structure as it is synthesized within the ribosome. Chaperones are molecules that assist protein folding.

(c)

Summary Introduction

To determine: The positions at which the substitutions are restricted to amino acids with negatively charged side chains. Also, to determine the amino acid that predominates each position.

Introduction:

Protein folding is a process, by which a protein molecule acquires biologically functional $\text{3-D}$ (three-dimensional) conformation from its random coiled structure. After translation, proteins have an unfolded linear chain of amino acids. This protein or polypeptide begins to fold into $\text{3-D}$ structure as it is synthesized within the ribosome. Chaperones are molecules that assist protein folding.

(d)

Summary Introduction

To determine: The position at which any amino acid can be occupied and the amino acid that appears most often.

Introduction:

Protein folding is a process, by which a protein molecule acquires biologically functional $\text{3-D}$ (three-dimensional) conformation from its random coiled structure. After translation, proteins have an unfolded linear chain of amino acids.. This protein or polypeptide begins to fold into $\text{3-D}$ structure as it is synthesized within the ribosome. Chaperones are molecules that assist protein folding.