Macromolecular Crowding Stabilizes the Molten Globule Form of Apomyoglobin with Respect to Both Cold and Heat Unfolding

Journal of Molecular Biology

Volumn 361, Issue 1, 2006, Pages 7-10

  McPhie, Peter ^a   Ni, Yi sheng ^a   Minton, Allen P ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

cold denaturation; excluded volume; molecular crowding; molten globule; protein stability

Indexed keywords

APOMYOGLOBIN; DEXTRAN; POLYMER; SODIUM CHLORIDE;

ADDITION REACTION; ARTICLE; CIRCULAR DICHROISM; COLD; CONCENTRATION (PARAMETERS); DATA ANALYSIS; HEAT; MACROMOLECULE; MOLECULAR DYNAMICS; MOLECULAR STABILITY; MOLECULAR WEIGHT; MOLTING; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE; THEORY; THERMAL STIMULATION;

EID: 33745909428     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.05.075     Document Type: Article

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