Document Detail


Simultaneous and multivariate alignment of protein sequences: correspondence between physicochemical profiles and structurally conserved regions (SCR).
MedLine Citation:
PMID:  1946318     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A general protein sequence alignment methodology for detecting a priori unknown common structural and functional regions is described. The method proposed in this paper is based on two basic requirements for a meaningful alignment. First, each sequence or segment of a sequence is characterized by a multivariate physicochemical profile. Second, the alignment is performed by considering all the sequences simultaneously, and the algorithm detects those regions that form a set of similar profiles. In order to test the structural meaning of the alignment obtained from the sequences, quantitative comparisons are performed with structurally conserved regions (SCR) determined from the X-ray structures of three serine proteases. Results suggest that the limits of the SCR may be predicted from the similarities between the physicochemical profiles of the sequences. The procedures are not completely automated. The final step requires a visual screening of alternative pathways in order to determine an optimal alignment.
Authors:
E Depiereux; E Feytmans
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Protein engineering     Volume:  4     ISSN:  0269-2139     ISO Abbreviation:  Protein Eng.     Publication Date:  1991 Aug 
Date Detail:
Created Date:  1991-12-13     Completed Date:  1991-12-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8801484     Medline TA:  Protein Eng     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  603-13     Citation Subset:  IM    
Affiliation:
Department of Biology, Facultés Universitaires Notre Dame de la Paix, Namur, Belgium.
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MeSH Terms
Descriptor/Qualifier:
Algorithms
Amino Acid Sequence
Molecular Sequence Data
Sequence Alignment / methods*
Serine Endopeptidases / chemistry
Chemical
Reg. No./Substance:
EC 3.4.21.-/Serine Endopeptidases

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


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