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Molecular model of human tropoelastin and implications of associated mutations

Author(s)
Yeo, Giselle C.; Baldock, Clair; Weiss, Anthony S.; Tarakanova, Anna; Buehler, Markus J
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Abstract
Protein folding poses unique challenges for large, disordered proteins due to the low resolution of structural data accessible in experiment and on the basis of short time scales and limited sampling attainable in computation. Such molecules are uniquely suited to accelerated-sampling molecular dynamics algorithms due to a flat-energy landscape. We apply these methods to report here the folded structure in water from a fully extended chain of tropoelastin, a 698-amino acid molecular precursor to elastic fibers that confer elasticity and recoil to tissues, finding good agreement with experimental data. We then study a series of artificial and disease-related mutations, yielding molecular mechanisms to explain structural differences and variation in hierarchical assembly observed in experiment. The present model builds a framework for studying assembly and disease and yields critical insight into molecular mechanisms behind these processes. These results suggest that proteins with disordered regions are suitable candidates for characterization by this approach. Keywords: tropoelastin; elastic fiber; structural protein; disordered protein; molecular dynamics
Date issued
2018-07
URI
http://hdl.handle.net/1721.1/120613
Department
Massachusetts Institute of Technology. Department of Civil and Environmental Engineering
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
Tarakanova, Anna et al. “Molecular Model of Human Tropoelastin and Implications of Associated Mutations.” Proceedings of the National Academy of Sciences 115, 28 (June 2018): 7338–7343 © 2018 National Academy of Sciences
Version: Final published version
ISSN
0027-8424
1091-6490

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