The Genetic Control of Tertiary Protein Structure: Studies With Model Systems

  1. Charles J. Epstein,
  2. Robert F. Goldberger, and
  3. Christian B. Anfinsen
  1. National Heart Institute, National Institutes of Health, Bethesda, Maryland

This extract was created in the absence of an abstract.

Excerpt

HYPOTHESIS CONCERNING DETERMINATION OF PROTEIN CONFIGURATION

At the present time it is generally assumed that most, if not all, proteins possess well-defined structures. This assumption is based on several kinds of evidence: (1) the finding that many proteins have unique amino acid sequences, with specific intrachain disulfide bonds; (2) the ability to determine the three-dimensional configuration (tertiary structure) and, in some instances, even portions of the amino acid sequence of proteins such as myoglobin and hemoglobin by X-ray crystallographic methods; (3) the highly reproducible physical-chemical properties of a large number of proteins; and (4) the great degree of configurational specificity which appears necessary for enzymic activity. When one considers the complexity of the tertiary structure of a “native” protein, it seems reasonable to inquire into how a newly-made protein arrives at its three-dimensional configuration.

The current theories of protein biosynthesis implicate linear macromolecules for storing and transmitting genetic information. Information...

| Table of Contents