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PMID: 4351801 Published · ppublish English Journal Article

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

Wetlaufer DB

Abstract

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 adding peptide chain segments that are close to the nucleus in aminoacid sequence. Such a process would generate three-dimensional (native) protein structures that contain separate regions of continuous peptide chain. Possible means of testing this hypothesis are discussed.

MeSH Terms
Albumins Chymotrypsin Immunoglobulins L-Lactate Dehydrogenase Malate Dehydrogenase Models, Structural Muramidase Myoglobin Pancreatic Elastase Papain Phosphoglycerate Kinase Phosphoric Monoester Hydrolases Protein Conformation Ribonucleases Rubredoxins Serum Albumin, Bovine Subtilisins Thermolysin Trypsin Trypsin Inhibitors
Chemicals
Albumins Immunoglobulins Myoglobin Rubredoxins Trypsin Inhibitors Serum Albumin, Bovine L-Lactate Dehydrogenase Malate Dehydrogenase Phosphoglycerate Kinase Ribonucleases Phosphoric Monoester Hydrolases Muramidase Subtilisins Chymotrypsin Pancreatic Elastase Trypsin Papain Thermolysin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Wetlaufer D B
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32 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1973-03-00
Pages
697-701
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433338
Subset
IM
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