Prediction of natively unfolded regions in protein chains.

Autor:	Galzitskaya, O. V., Garbuzynskiy, S. O., Lobanov, M. Yu.
Předmět:	PROTEINS AMINO acids PROTEIN folding PROTEIN conformation ALGORITHMS
Zdroj:	Molecular Biology; Mar2006, Vol. 40 Issue 2, p298-304, 7p, 3 Charts, 3 Graphs
Abstrakt:	Analysis showed that the globular or natively unfolded state of a protein can be inferred not only from a lower hydrophobicity or a higher charge, but also from the average environment density (average number of close residues located within a certain distance of a given one) of its residues. A database of 6626 protein structures was used to construct a statistical scale of the average number of close residues in globular structures for the 20 amino acids. The portion of false predictions in distinguishing between 80 globular and 90 natively unfolded proteins was 11% with the new scale and 17% with a hydrophobicity scale. The new scale proved suitable for predicting the folded or unfolded state for native proteins or the natively unfolded regions for protein chains. In comparisons with the available algorithms, the new method yielded the highest portion of true predictions (87 and 77% with averaging over residues and over proteins, respectively). [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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