Cavities determine the pressure unfolding of proteins

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

Volumn 109, Issue 18, 2012, Pages 6945-6950

  Roche, Julien ^a   Caro, Jose A ^b   Norberto, Douglas R ^a,c   Barthe, Philippe ^a   Roumestand, Christian ^a   Schlessman, Jamie L ^d   Garcia, Angel E ^e   García Moreno, Bertrand E ^b   Royer, Catherine A ^a  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CAMPINAS   (Brazil)

^d UNITED STATES NAVAL ACADEMY   (United States)

^e Research Rensselaer Polytechnic Institute   (United States)

Author keywords

Energy landscape; Fluorescence; Volume change

Indexed keywords

NUCLEASE;

ARTICLE; CRYSTAL STRUCTURE; EQUILIBRIUM CONSTANT; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRESSURE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; STAPHYLOCOCCUS; WATER PERMEABILITY;

AMINO ACID SUBSTITUTION; BIOPHYSICAL PHENOMENA; CRYSTALLOGRAPHY, X-RAY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; SOLVENTS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; UNFOLDED PROTEIN RESPONSE; WATER;

EID: 84860829715     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200915109     Document Type: Article

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