Influence of Organization of Native Protein Structure on Its Folding: Modeling of the Folding of α-Helical Proteins

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A. V. Glyakina¹ and O. V. Galzitskaya^2*

¹Institute of Mathematical Problems of Biology, Russian Academy of Sciences, ul. Institutskaya 4, 142290 Pushchino, Moscow Region, Russia

²Institute of Protein Research, Russian Academy of Sciences, ul. Institutskaya 4, 142290 Pushchino, Moscow Region, Russia; fax: (84967) 318-435; E-mail: ogalzit@vega.protres.ru

^* To whom correspondence should be addressed.

Received March 31, 2010; Revision received April 14, 2010

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An important question that is addressed here is whether the modeling of protein folding can catch the difference between the folding of proteins with similar structures but with different folding mechanisms. In this work, the modeling of folding of four α-helical proteins from the homeodomain family, which are similar in size, was done using the Monte Carlo and dynamic programming methods. A frequently observed order of folding of α-helices for each protein was determined using the Monte Carlo method. A correlation between the experimental folding rate and the number of Monte Carlo steps was also demonstrated. Amino acid residues that are important for the folding were determined using the dynamic programming method. The defined regions correlate with the order of folding of secondary-structure elements in the proteins both in experiments and in modeling.

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KEY WORDS: protein folding, folding intermediates, folding nuclei, nucleation mechanism, diffusion–collision mechanism

DOI: 10.1134/S0006297910080079

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