Document Detail

Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association.
MedLine Citation:
PMID:  9232644     Owner:  NLM     Status:  MEDLINE    
A hydrophobic folding unit cutting algorithm, originally developed for dissecting single-chain proteins, has been applied to a dataset of dissimilar two-chain protein-protein interfaces. Rather than consider each individual chain separately, the two-chain complex has been treated as a single chain. The two-chain parsing results presented in this work show hydrophobicity to be a critical attribute of two-state versus three-state protein-protein complexes. The hydrophobic folding units at the interfaces of two-state complexes suggest that the cooperative nature of the two-chain protein folding is the outcome of the hydrophobic effect, similar to its being the driving force in a single-chain folding. In analogy to the protein-folding process, the two-chain, two-state model complex may correspond to the formation of compact, hydrophobic nuclei. On the other hand, the three-state model complex involves binding of already folded monomers, similar to the association of the hydrophobic folding units within a single chain. The similarity between folding entities in protein cores and in two-state protein-protein interfaces, despite the absence of some chain connectivities in the latter, indicates that chain linkage does not necessarily affect the native conformation. This further substantiates the notion that tertiary, non-local interactions play a critical role in protein folding. These compact, hydrophobic, two-chain folding units, derived from structurally dissimilar protein-protein interfaces, provide a rich set of data useful in investigations of the role played by chain connectivity and by tertiary interactions in studies of binding and of folding. Since they are composed of non-contiguous pieces of protein backbones, they may also aid in defining folding nuclei.
C J Tsai; R Nussinov
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  6     ISSN:  0961-8368     ISO Abbreviation:  Protein Sci.     Publication Date:  1997 Jul 
Date Detail:
Created Date:  1997-09-11     Completed Date:  1997-09-11     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1426-37     Citation Subset:  IM    
Laboratory of Mathematical Biology, NCI-FCRDC, Frederick, Maryland 21702, USA.
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MeSH Terms
Models, Chemical
Models, Molecular
Protein Binding
Protein Conformation*
Protein Folding*
Grant Support

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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