Sequence patterns associated with disordered regions in proteins.
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.
Lise
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Department of Biochemistry and Molecular Biology, University College London, London, United Kingdom. lise@biochem.ucl.ac.uk <lise@biochem.ucl.ac.uk>
Jones
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DT
D000595:Amino Acid Sequence / Q000235:genetics*; D003198:Computer Simulation; D030562:Databases, Protein; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary / Q000235:genetics; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*
D011506:Proteins