NMR study of the cataract-linked P23T mutant of human γD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility

Biochemical and Biophysical Research Communications

Volumn 382, Issue 1, 2009, Pages 196-199

  Pande, Ajay ^a   Zhang, Jianchao ^a   Banerjee, Priya R ^a   Puttamadappa, Shadakshara S ^a   Shekhtman, Alexander ^a   Pande, Jayanti ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Cataract; Chemical shift; Crystallin; Mutation; NMR

Indexed keywords

CRYSTALLIN; GAMMA D CRYSTALLIN; PROLINE; THREONINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATARACT; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENE; GENE MUTATION; HUMAN; HYDROPHOBICITY; LIQUID LIQUID EXTRACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; P23T GENE; PHASE TRANSITION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; SOLUBILITY;

CATARACT; CRYSTALLINS; HUMANS; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; SOLUBILITY; THREONINE;

EID: 63149088162     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.007     Document Type: Article

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