Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 58, Issue 1, Pages 144-150Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.20279
Keywords
disordered proteins; sequence patterns; structure prediction; structure-function paradigm
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Funding
- Medical Research Council [G90/70] Funding Source: Medline
- MRC [G90/70] Funding Source: UKRI
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The relationship between amino acid sequence and intrinsic disorder in proteins is investigated. Two databases, one of disordered proteins and the other of globular proteins, are analyzed and compared in order to extract simple sequence patterns of a few amino acids or amino acid properties that characterize disordered segments. It is found that a number of reliable, nonrandom associations exists. In particular, two types of patterns appear to be recurrent: a proline-rich pattern and a (positively or negatively) charged pattern. These results indicate that local sequence information can determine disordered regions in proteins. The derived patterns provide some insights into the physical reasons for disordered structures. They should also be helpful in improving currently available prediction methods. (C) 2004 Wiley-Liss, Inc.
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