Protein Folding: The Stepwise Assembly of Foldon Units

Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is composed of five foldon units that continually unfold and refold even under native conditions. Folding proceeds by the stepwise assembly of the foldon units rather than one amino acid at a time. The folding pathway is de...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2005-03, Vol.102 (13), p.4741-4746
Main Authors: Maity, Haripada, Maity, Mita, Mallela M. G. Krishna, Mayne, Leland, Englander, S. Walter
Format: Article
Language:English
Subjects:
Amides
Animals
Biochemistry
Biological Sciences
Biophysics
Color semiotics
Cytochromes c - chemistry
Deuterium Exchange Measurement
Free energy
Horses - metabolism
Hydrogen
Isotherms
Kinetics
Melting
Models, Molecular
Protein Conformation
Protein Folding
Protein refolding
Protein Subunits - chemistry
Proteins
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Summary:Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is composed of five foldon units that continually unfold and refold even under native conditions. Folding proceeds by the stepwise assembly of the foldon units rather than one amino acid at a time. The folding pathway is determined by a sequential stabilization process; previously formed foldons guide and stabilize subsequent foldons to progressively build the native protein. Four other proteins have been found to show similar behavior. These results support stepwise protein folding pathways through discrete intermediates.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0501043102