Solution of Levinthal’s paradox is possible at the level of the formation and assembly of protein secondary structures
- Авторы: Finkelstein A.V.1, Garbuzynskiy S.O.1
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Учреждения:
- Institute of Protein Research
- Выпуск: Том 61, № 1 (2016)
- Страницы: 1-5
- Раздел: Molecular Biophysics
- URL: https://ogarev-online.ru/0006-3509/article/view/151886
- DOI: https://doi.org/10.1134/S0006350916010085
- ID: 151886
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Аннотация
The complete volume of a protein’s conformation space is smaller by many orders of magnitude at the level of secondary-structure elements as compared with the conformation of amino-acid residues. According to Levinthal’s estimate, the latter is ~102L, with L being the number of residues in the chain, while the former, at the level of secondary structures, increases no faster than ~LN with N being the number of the secondary-structure elements. N is approximately L/15 according to the statistics of protein structures. This drastic decrease in the exponent (L/15 instead of 2L) considerably reduces the sampling space and explains the reason that sampling of the conformation space at the level of secondary-structure elements does not prevent the protein chain from finding its most stable structure.
Об авторах
A. Finkelstein
Institute of Protein Research
Автор, ответственный за переписку.
Email: afinkel@vega.protres.ru
Россия, ul. Institutskaya 4, Pushchino, Moscow oblast, 142290
S. Garbuzynskiy
Institute of Protein Research
Email: afinkel@vega.protres.ru
Россия, ul. Institutskaya 4, Pushchino, Moscow oblast, 142290
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