Document Detail


Functionally acceptable substitutions in two alpha-helical regions of lambda repressor.
MedLine Citation:
PMID:  2199970     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A method of targeted random mutagenesis has been used to investigate the informational content of 25 residue positions in two alpha-helical regions of the N-terminal domain of lambda repressor. Examination of the functionally allowed sequences indicates that there is a wide range in tolerance to amino acid substitution at these positions. At positions that are buried in the structure, there are severe limitations on the number and type of residues allowed. At most surface positions, many different residues and residue types are tolerated. However, at several surface positions there is a strong preference for hydrophilic amino acids, and at one surface position proline is absolutely conserved. The results reveal the high level of degeneracy in the information that specifies a particular protein fold.
Authors:
J F Reidhaar-Olson; R T Sauer
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proteins     Volume:  7     ISSN:  0887-3585     ISO Abbreviation:  Proteins     Publication Date:  1990  
Date Detail:
Created Date:  1990-09-11     Completed Date:  1990-09-11     Revised Date:  2008-08-14    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  306-16     Citation Subset:  IM    
Affiliation:
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
DNA-Binding Proteins*
Escherichia coli / genetics*
Membrane Proteins
Molecular Sequence Data
Monte Carlo Method
Mutation
Protein Conformation
Repressor Proteins* / genetics
Transcription Factors* / genetics
Viral Proteins
Viral Regulatory and Accessory Proteins
Grant Support
ID/Acronym/Agency:
AI-15706/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Membrane Proteins; 0/Repressor Proteins; 0/Transcription Factors; 0/Viral Proteins; 0/Viral Regulatory and Accessory Proteins; 0/phage repressor proteins

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


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