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CHAPTER   4   Myoglobin and Hemoglobin: A Study of
Protein Structure and Function


Most of an organism’s genetic information directs the synthesis of proteins, which are the molecules that carry out virtually all the metabolic work of the organism. In this chapter, we take a close look at the oxygen-binding proteins myoglobin and hemoglobin. Myoglobin is an intracellular protein that gives vertebrate muscles their red color, and hemoglobin is the major protein of red blood cells. These two proteins provide a wealth of information on how molecular structure is related to biological function. The chapter first looks at the chemical properties of the amino acid components of proteins, along with methods for determining the sequence of amino acids in a protein. Next comes a discussion of how the protein backbone and side chains fold into a unique three-dimensional shape stabilized by noncovalent forces. Detailed structural information about proteins such as myoglobin and hemoglobin leads to an understanding of how these proteins bind oxygen and how their physiological function is modulated by other factors. A comparison of the molecular structures of these protein also sheds light on how proteins evolve.

Amino Acids Biomolecular Tour: The proteins in all organisms are built from a set of 20 standard amino acids.
Protein Secondary Structure Biomolecular Tour: On its way to folding into its native conformation, a string of amino acids twists and turns so that its backbone assumes a variety of stable secondary structures that include helices, sheets, turns, and loops.
Myoglobin and Hemoglobin Biomolecular Tour: Myoglobin and hemoglobin are well-characterized models for illustrating the principles of protein structure, dynamics, and physiological function.
Related Links Chapter 4 Quiz
Web Links
Biomolecular Structures
Student Activity: Proteomics
Student Activity: Phylogenetic Trees

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