Biophysical Properties of γC-Crystallin in Human and Mouse Eye Lens: The Role of Molecular Dipoles

Journal of Molecular Biology

Volumn 372, Issue 1, 2007, Pages 205-222

  Purkiss, Andrew G ^a   Bateman, Orval A ^a   Wyatt, Keith ^b   Wilmarth, Phillip A ^c   David, Larry L ^c   Wistow, Graeme J ^b   Slingsby, Christine ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b NATIONAL EYE INSTITUTE   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

crystallin; cysteine; eye lens; protein solubility; solution interactions

Indexed keywords

CRYSTALLIN; GAMMA C CRYSTALLIN; UNCLASSIFIED DRUG; CRYGC PROTEIN, HUMAN; GAMMA CRYSTALLIN; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DIPOLE; HUMAN; LENS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DOG; GENETICS; GUINEA PIG; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; MOUSE; PHYSIOLOGY; POINT MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SOLUBILITY;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; DOGS; GAMMA-CRYSTALLINS; GUINEA PIGS; HUMANS; LENS, CRYSTALLINE; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY;

EID: 34547665320     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.049     Document Type: Article

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