Sequence determinants of protein architecture

ABSTRACT Delineation of the relationship between sequence and structure in proteins has proven elusive. Most studies of this problem use alignment methods and other approaches based on the characteristics of individual residues. It is demonstrated herein that the sequence‐structure relationship is d...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2013-10, Vol.81 (10), p.1681-1685
Main Author: Rackovsky, S.
Format: Article
Language:English
Subjects:
Computational Biology - methods
Databases, Factual
distant homologies
fold detection
Fourier Analysis
Protein Conformation
Protein Folding
Proteins - chemistry
Proteins - metabolism
Sequence Analysis, Protein - methods
sequence-structure relationships
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Summary:ABSTRACT Delineation of the relationship between sequence and structure in proteins has proven elusive. Most studies of this problem use alignment methods and other approaches based on the characteristics of individual residues. It is demonstrated herein that the sequence‐structure relationship is determined in significant part by global characteristics of sequence organization. Information encoded in complete sequences is required to distinguish proteins in different architectural groups. It is found that the statistically significant differences between sequences encoding different architectures are encoded in a surprisingly small set of low‐wave‐number sequence periodicities. It would therefore appear that unexpected simplicity in an appropriately defined Fourier space may be an inherent characteristic of the sequences of folded proteins. Proteins 2013; 81:1681–1685. © 2013 Wiley Periodicals, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.24328