Is there a single pathway for the folding of a polypeptide chain?
AUTOR(ES)
Harrison, S C
RESUMO
We argue that folding of the compact domains of proteins can occur with adequate rapidity in the absence of a unique directed mechanism, provided that native-like local structure dominates the folding process. We further suggest that the evolution of amino acid sequences should favor multiple paths to the folded state. Existing physicochemical and mutational data are not inconsistent with a many-pathway model. The analogy of a jigsaw puzzle, with multiple routes to a unique solution, appears to be particularly apt.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=397927Documentos Relacionados
- EVIDENCE FOR MULTIPLE GENE CONTROL OF A SINGLE POLYPEPTIDE CHAIN: THE HEAVY CHAIN OF RABBIT IMMUNOGLOBULIN
- Is there proofreading during polypeptide synthesis?
- Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding
- Heterogeneity of rabbit endogenous pyrogens is not attributable to glycosylated variants of a single polypeptide chain.
- Actin compliance: are you pulling my chain?