Cold denaturation and aggregation: A comparative NMR study of titin i28 in bulk and in a confined environment

Journal of the American Chemical Society

Volumn 131, Issue 33, 2009, Pages 11662-11663

  Sanfelice, Domenico ^a   Tancredi, Teodorico ^b   Politou, Anastasia ^c   Pastore, Annalisa ^e   Temussi, Piero A ^a,d  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF IOANNINA   (Greece)

^d NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^e NONE

Author keywords

[No Author keywords available]

Indexed keywords

COLD DENATURATION; CONFINED ENVIRONMENT; HIGH TEMPERATURE; NMR STUDIES; PHYSIOLOGICAL CONDITION; POLYACRYLAMIDE GELS; SUB-ZERO TEMPERATURES; TEMPERATURE RANGE; THERMAL STABILITY; THERMODYNAMICS PARAMETERS;

GELATION; NUCLEAR MAGNETIC RESONANCE; POLYETHYLENE GLYCOLS; POLYETHYLENE OXIDES; PROTEINS; THERMODYNAMIC STABILITY;

DENATURATION;

MUSCLE PROTEIN; PROTEIN TITIN I28; UNCLASSIFIED DRUG;

ARTICLE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY;

ACRYLIC RESINS; COLD TEMPERATURE; MAGNETIC RESONANCE SPECTROSCOPY; MUSCLE PROTEINS; POLYETHYLENE GLYCOLS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN KINASES; PROTEIN STABILITY; THERMODYNAMICS;

EID: 69049088797     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja904462n     Document Type: Article

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