The C-peptide Helix from Ribonuclease A Considered as an Autonomous Folding Unit

  1. K.R. Shoemaker,
  2. R. Fairman,
  3. P.S. Kim*,
  4. E.J. York,
  5. J.M. Stewart, and
  6. R.L. Baldwin
  1. Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305; Department of Biochemistry, University of Colorado School of Medicine, Denver, Colorado 80262

This extract was created in the absence of an abstract.

Excerpt

One of the basic goals of work on the mechanism of protein folding is to define autonomous folding units: those individual segments of a protein which, if excised, contain sufficient structural information to specify their own folding. Surprisingly little is known about this subject. A common opinion is that entire domains are the units of folding. A domain is defined as (1) a continuous segment of polypeptide chain that is folded on itself, as judged by inspection of the protein's X-ray structure, and (2) a folded segment that makes only marginal contacts with neighboring segments. Domains are usually found to contain 100–150 amino acid residues. The nature of protein structure is such that a domain can be divided into two subdomains and each subdomain can be further divided, if the definition of a subdomain is based on part 1 above (Rose 1979), without part 2.

Autonomous folding units might, however,...

  • * Present address: Whitehead Institute, Nine Cambridge Center, Cambridge, Massachusetts 02142.

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