High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin

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

Volumn 110, Issue 5, 2013, Pages

  Vajpai, Navratna ^a,b   Nisius, Lydia ^a   Wiktor, Maciej ^a   Grzesiek, Stephan ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b ASTRAZENECA   (United Kingdom)

Author keywords

Heteronuclear NMR; Protein dynamics; Protein unfolding; Thermodynamics

Indexed keywords

ALCOHOL; UBIQUITIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; COLD; HYPERBARISM; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TRANSITION TEMPERATURE;

COLD TEMPERATURE; ETHANOL; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; METHANOL; MODELS, MOLECULAR; PRESSURE; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; THERMODYNAMICS; UBIQUITIN;

EID: 84873162609     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212222110     Document Type: Article

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