Bacterial Proteins Fold Faster than Eukaryotic Proteins with Simple Folding Kinetics

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O. V. Galzitskaya^1*, N. S. Bogatyreva¹, and A. V. Glyakina²

¹Institute of Protein Research, Russian Academy of Sciences, Institutskaya ul. 4, 142290 Pushchino, Moscow Region, Russia; fax: (4967) 318-435; E-mail: ogalzit@vega.protres.ru

²Institute of Mathematical Problems of Biology, Russian Academy of Sciences, Institutskaya ul. 4, 142290 Pushchino, Moscow Region, Russia

^* To whom correspondence should be addressed.

Received April 28, 2010; Revision received September 16, 2010

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Protein domain frequency and distribution among kingdoms was statistically analyzed using the SCOP structural database. It appeared that among chosen protein domains with the best resolution, eukaryotic proteins more often belong to α-helical and β-structural proteins, while proteins of bacterial origin belong to α/β structural class. Statistical analysis of folding rates of 73 proteins with known experimental data revealed that bacterial proteins with simple kinetics (23 proteins) exhibit a higher folding rate compared to eukaryotic proteins with simple folding kinetics (27 proteins). Analysis of protein domain amino acid composition showed that the frequency of amino acid residues in proteins of eukaryotic and bacterial origin is different for proteins with simple and complex folding kinetics.

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KEY WORDS: “all-or-none” transition, eukaryotic and bacterial proteins, folding intermediates, folding rate, protein folding

DOI: 10.1134/S000629791102009X

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