Increase in surface hydrophobicity of the cataract-associated P23T mutant of human γd-Crystallin is responsible for its dramatically lower, retrograde solubility

Biochemistry

Volumn 49, Issue 29, 2010, Pages 6122-6129

  Pande, Ajay ^a   Ghosh, Kalyan S ^a   Banerjee, Priya R ^a   Pande, Jayanti ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPIC INTERACTION; CATARACT FORMATION; CHEMICAL PROBES; CRYSTALLIN; HYDROPHOBIC PROTEIN; IN-VITRO; MODELING STUDIES; MOLECULAR BASIS; MUTANT PROTEINS; N-TERMINAL DOMAINS; PROTEIN CLUSTERS; PROTEIN-PROTEIN INTERACTIONS; RETROGRADE SOLUBILITY; SURFACE HYDROPHOBICITY;

ANISOTROPY; BIOCHEMISTRY; HYDROPHOBICITY; SEMICONDUCTING GALLIUM COMPOUNDS; SOLUBILITY;

PROTEINS;

GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; MUTANT PROTEIN; PROLINE; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; CATARACT; HUMAN; HUMAN CELL; HYDROPHOBICITY; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLUBILITY;

CATARACT; GAMMA-CRYSTALLINS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; PROLINE; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; THREONINE;

EID: 77954821049     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100664s     Document Type: Article

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