Structure and mechanism of maximum stability of isolated alpha-helical protein domains at a critical length scale
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10189_2013_Article_9867.pdf
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Author(s)
Qin, Zhao
Fabre, Andrea
Buehler, Markus J
Date Issued
May 2013
Journal
The European Physical Journal E
Publisher
Springer Berlin Heidelberg
Citation
Qin, Zhao, Andrea Fabre, and Markus J. Buehler. “Structure and Mechanism of Maximum Stability of Isolated Alpha-Helical Protein Domains at a Critical Length Scale.” The European Physical Journal E 36.5 (2013): n. pag.
Version
Author's final manuscript
Abstract
The stability of alpha helices is important in protein folding, bioinspired materials design, and controls many biological properties under physiological and disease conditions. Here we show that a naturally favored alpha helix length of 9 to 17 amino acids exists at which the propensity towards the formation of this secondary structure is maximized. We use a combination of thermodynamical analysis, well-tempered metadynamics molecular simulation and statistical analyses of experimental alpha helix length distributions and find that the favored alpha helix length is caused by a competition between alpha helix folding, unfolding into a random coil and formation of higher-order tertiary structures. The theoretical result is suggested to be used to explain the statistical distribution of the length of alpha helices observed in natural protein structures. Our study provides mechanistic insight into fundamental controlling parameters in alpha helix structure formation and potentially other biopolymers or synthetic materials. The result advances our fundamental understanding of size effects in the stability of protein structures and may enable the design of de novo alpha-helical protein materials.
MIT Department
Massachusetts Institute of Technology. Center for Materials Science and Engineering
Massachusetts Institute of Technology. Center for Computational Engineering
Massachusetts Institute of Technology. Department of Chemical Engineering
Massachusetts Institute of Technology. Department of Civil and Environmental Engineering
Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics
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DOI of Published Version
https://doi.org/10.1140/epje/i2013-13053-8
