Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

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

Volumn 108, Issue 52, 2011, Pages 21057-21062

  De Simone, Alfonso ^a   Dhulesia, Anne ^b   Soldi, Gemma ^e   Vendruscolo, Michele ^b   Hsu, Shang Te Danny ^c,d   Chiti, Fabrizio ^e   Dobson, Christopher M ^b  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^d INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^e UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Avoidance of protein aggregation; Free energy barriers; Molecular simulations; Protein misfolding

Indexed keywords

ACPDRO2 PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; ENERGY; ENERGY TRANSFER; ENZYME ACTIVITY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SOLUBILITY; SURFACE PROPERTY;

ACID ANHYDRIDE HYDROLASES; ANIMALS; DROSOPHILA MELANOGASTER; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; SOLUBILITY;

DROSOPHILA MELANOGASTER;

EID: 84855438639     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1112197108     Document Type: Article

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