Document Detail


The effect of neighboring charges on the helix forming ability of charged amino acids in proteins.
MedLine Citation:
PMID:  1177494     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been found that the fraction of glutamic acid residues which are helical in proteins is larger than might be expected from the experimentally determined value of the helical stability constants of glutamic acid. In order to understand this difference, the effect of neighboring charged side chains on the glutamic acid residues in proteins of known structure is examined. It is found that a positively charged side chain four residues away from a glutamic acid greatly enhances its probability to be helical. Similar results are obtained for aspartic acid, lysine, arginine, and histidine.
Authors:
F R Maxfield; H A Scheraga
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Macromolecules     Volume:  8     ISSN:  0024-9297     ISO Abbreviation:  Macromolecules     Publication Date:    1975 Jul-Aug
Date Detail:
Created Date:  1976-01-02     Completed Date:  1976-01-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0365316     Medline TA:  Macromolecules     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  491-3     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids
Aspartic Acid
Binding Sites
Glutamates
Kinetics
Mathematics
Protein Conformation*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Glutamates; 56-84-8/Aspartic Acid

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


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