While according to the thermodynamic hypothesis, protein folding reproducibility is ensured by the assumption that the native state corresponds to the minimum of the free energy in normal cellular conditions, here, the VES kinetic mechanism for folding in vivo is described according to which the nascent chain of all proteins is helical and the first and structure defining step in the folding pathway is the bending of that initial helix around a particular amino acid site. Molecular dynamics simulations are presented which indicate both the viability of this mechanism for folding and its limitations in the presence of a Markovian thermal bath. An analysis of a set of protein structures formed only of helices and loops suggests that bending sites are correlated with regions bounded, on the N-side, by positively charged amino acids like Lysine and Histidine and on the C-side by negatively charged amino acids like Aspartic acid.
J. Aramini, S. Sharma, Y. Huang, G. Swapna, C. Ho, K. Shetty, K. Cunningham, L. Ma, L. Zhao, L. Owens, M. Jiang, R. Xiao, J. Liu, M. Baran, T. Acton, B. Rost, G. Montelione. Proteins72, 526 (2008).1843175010.1002/prot.22064)| false
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