Are the Same or Different Amino Acid Residues Responsible for Correct and Incorrect Protein Folding?

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O. V. Galzitskaya

Institute of Protein Research, Russian Academy of Sciences, ul. Institutskaya 4, 142290 Pushchino, Moscow Region, Russia; fax: (495) 632-7871; E-mail: ogalzit@vega.protres.ru

Received August 13, 2008

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It has been shown for 20 proteins that amino acid residues included into the protein folding nucleus, determined experimentally, are often involved in the theoretically determined amyloidogenic fragments. For 18 proteins, Φ-values indicative of the extent of residue involvement into the folding nucleus are on average higher for amino acid residues within amyloidogenic regions. Amyloidogenic fragments were predicted for 20 proteins by two methods chosen from four on the basis of comparison of prediction of amyloidogenic regions known from experimental data. Since theoretical folding nuclei are detected by the protein three-dimensional structure and amyloidogenic regions by the protein chain primary structure, the detected regularity makes possible predictions of folding nucleation sites on the basis of amino acid sequence.

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KEY WORDS: folding nucleus, amyloid fibril, globular proteins, amyloidogenic regions, FoldUnfold, Tango, Zyggregator

DOI: 10.1134/S0006297909020096

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