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Molecular model of human tropoelastin and implications of associated mutations.

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.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Tarakanova A,Yeo GC,Baldock C,Weiss AS,Buehler MJ

doi

10.1073/pnas.1801205115

subject

Has Abstract

pub_date

2018-07-10 00:00:00

pages

7338-7343

issue

28

eissn

0027-8424

issn

1091-6490

pii

1801205115

journal_volume

115

pub_type

杂志文章

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