Revealing the nature of the native state ensemble through cold denaturation

Biochemistry

Volumn 45, Issue 34, 2006, Pages 10163-10174

  Whitten, Steven T ^a   Kurtz, Andrew J ^a   Pometun, Maxim S ^b   Wand, A Joshua ^b,c   Hilser, Vincent J ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PERTURBATION TECHNIQUES; THERMODYNAMIC PROPERTIES; WATER;

FOLDED STATES; FREEZING POINT; PROTEIN ENSEMBLE;

PROTEINS;

PROTEIN; UBIQUITIN;

ARTICLE; ENERGY; LOW TEMPERATURE PROCEDURES; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ANIMALS; COLD; CYTOCHROMES C; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; UBIQUITIN;

EID: 33748663531     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060855+     Document Type: Article

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