Nucleation, Rapid Folding, and Globular Intrachain Regions in Proteins

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Nucleation, rapid folding, and globular intrachain regions in proteins.

Distinct structural regions have been found in several globular proteins composed of single polypeptide chains. The existence of such regions and the continuity of peptide chain within them, coupled with kinetic arguments, suggests that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules. A nucleus can grow rapidly by a...

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Estimations of the size of nucleation regions in globular proteins.

Folding of many single-domain proteins has been described using the nucleation-collapse (NC) mechanism. According to NC, folding (formation of secondary structures and tertiary interactions) and chain collapse occur synchronously upon formation of native-like structures involving a critical number of residues. Using simple nucleation theory together with structure-based thermodynamic data, the ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1973

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.70.3.697