Deamidation alters the structure and decreases the stability of human lens βA3-crystallin

Biochemistry

Volumn 46, Issue 30, 2007, Pages 8861-8871

  Takata, Takumi ^a   Oxford, Julie T ^b   Brandon, Theodore R ^a   Lampi, Kirsten J ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b BOISE STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABERRANT CELLULAR DEBRIS; BLINDNESS; CATARACTS; PRECIPITATED LENS PROTEINS;

CRYSTALLINE MATERIALS; DEVELOPING COUNTRIES; LIGHT SCATTERING; PRECIPITATION (CHEMICAL); PROTEINS;

LENSES;

BETA A3 CRYSTALLIN; BETA CRYSTALLIN; GLUTAMIC ACID; LENS PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BLINDNESS; CARBOXY TERMINAL SEQUENCE; CATARACT; CIRCULAR DICHROISM; DEAMINATION; DENATURATION; DEVELOPING COUNTRY; LENS; NUCLEOTIDE SEQUENCE; PRECIPITATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; ULTRAVIOLET SPECTROSCOPY; WORLD HEALTH ORGANIZATION;

AMINO ACID SUBSTITUTION; BETA-CRYSTALLIN A CHAIN; CHROMATOGRAPHY, ION EXCHANGE; CIRCULAR DICHROISM; DIMERIZATION; GLUTAMIC ACID; GLUTAMINE; HUMANS; LENS, CRYSTALLINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PRECIPITATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SCATTERING, RADIATION; UREA;

EID: 34547631078     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700487q     Document Type: Article

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