Structure and mechanism of maximum stability of isolated alpha-helical protein domains at a critical length scale

Structure and mechanism of maximum stability of isolated alpha-helical protein domains at a critical length scale

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...

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Bibliographic Details
Main Authors: Qin, Zhao (Contributor), Fabre, Andrea (Contributor), Buehler, Markus J (Contributor)
Other Authors: Massachusetts Institute of Technology. Center for Materials Science and Engineering (Contributor), Massachusetts Institute of Technology. Center for Computational Engineering (Contributor), Massachusetts Institute of Technology. Department of Chemical Engineering (Contributor), Massachusetts Institute of Technology. Department of Civil and Environmental Engineering (Contributor), Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics (Contributor)
Format: Article
Language:English
Published: Springer Berlin Heidelberg, 2016-10-06T22:29:44Z.
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