Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides-Reference-Cited by-同舟云学术

Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides

Published:2013-02-20 Issue:5 Volume:99 Page:292-313
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Salvi Anna M.,Moscarelli Pasquale,Bochicchio Brigida,Lanza Giuseppe,Castle James E.

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.22160/fullpdf

Reference75 articles.

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3. Protein Folding and Misfolding on Surfaces

4. Hydration Effects on the HET-s Prion and Amyloid-β Fibrillous Aggregates, Studied with Three-Dimensional Molecular Theory of Solvation

5. Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding

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