Chapter 10, Problem 10.28PP

(a)

Summary Introduction

To explain:

Where these amino acids in myoglobin are to be located in the tertiary structure of the protein.

Introduction:

Myoglobin is a protein which consists of ${}_{}153$ amino acids. It is a monomeric protein which consists of eight alpha helices which are coiled together to form the folded structure of the molecule. It contains a heme group containing iron which binds to the oxygen atom and supplies it to the muscles of the body. This interaction is stabilized by the presence of histidine amino acids present in the backbone of the protein chain.

(b)

Summary Introduction

To explain:

Where the non-polar side chains are present in the myoglobin molecule.

Introduction:

Myoglobin is a protein which consists of ${}_{}153$ amino acids. It is a monomeric protein which consists of eight alpha helices which are coiled together to form the folded structure of the molecule. It contains a heme group containing iron which binds to the oxygen atom and supplies it to the muscles of the body. This interaction is stabilized by the presence of histidine amino acids present in the backbone of the protein chain.

(c)

Summary Introduction

To determine:

Whether myoglobin is more or less soluble in water as compared to a protein composed mainly of non-polar amino acids.

Introduction:

Myoglobin is a protein which consists of ${}_{}153$ amino acids. It is a monomeric protein which consists of eight alpha helices which are coiled together to form the folded structure of the molecule. It contains a heme group containing iron which binds to the oxygen atom and supplies it to the muscles of the body. This interaction is stabilized by the presence of histidine amino acids present in the backbone of the protein chain.