@article{
 title = {The liquid structure of elastin},
 type = {article},
 year = {2017},
 volume = {6},
 id = {662712f7-afaf-3d7e-ad96-b4ab3721ffa7},
 created = {2018-06-08T17:39:27.615Z},
 file_attached = {false},
 profile_id = {0633c91d-b6d5-3fcd-9fa3-6021f99f2c58},
 last_modified = {2018-06-08T17:39:27.615Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {© Rauscher and Pomès. The protein elastin imparts extensibility, elastic recoil, and resilience to tissues including arterial walls, skin, lung alveoli, and the uterus. Elastin and elastin-like peptides are hydrophobic, disordered, and undergo liquid-liquid phase separation upon self-assembly. Despite extensive study, the structure of elastin remains controversial. We use molecular dynamics simulations on a massive scale to elucidate the structural ensemble of aggregated elastin-like peptides. Consistent with the entropic nature of elastic recoil, the aggregated state is stabilized by the hydrophobic effect. However, self-assembly does not entail formation of a hydrophobic core. The polypeptide backbone forms transient, sparse hydrogen-bonded turns and remains significantly hydrated even as self-assembly triples the extent of non-polar side chain contacts. Individual chains in the assembly approach a maximally-disordered, melt-like state which may be called the liquid state of proteins. These findings resolve long-standing controversies regarding elastin structure and function and afford insight into the phase separation of disordered proteins.},
 bibtype = {article},
 author = {Rauscher, S. and Pomès, R.},
 doi = {10.7554/eLife.26526},
 journal = {eLife}
}

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