Deamidation in human lens βB2-crystallin destabilizes the dimer

Biochemistry

Volumn 45, Issue 10, 2006, Pages 3146-3153

  Lampi, Kirsten J ^a   Amyx, Kencee K ^a   Ahmann, Petra ^a   Steel, Eric A ^b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b SHRINERS HOSPITAL FOR CHILDREN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLINE MATERIALS; DIMERS; LIGHT SCATTERING; MONOMERS; MUTAGENESIS; STABILIZATION; SUBSTITUTION REACTIONS; TRANSPARENCY; UREA;

CRITICAL SITES; DEAMIDATION; DOUBLE MUTANT; HUMAN LENS;

LENSES;

BETA CRYSTALLIN; BETAB2 CRYSTALLIN; DIMER; GLUTAMIC ACID; MONOMER; MUTANT PROTEIN; UNCLASSIFIED DRUG; UREA;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; DEAMINATION; DIMERIZATION; HUMAN; IN VITRO STUDY; LENS; LIFESPAN; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

ARGININE; BETA-CRYSTALLIN B CHAIN; CIRCULAR DICHROISM; CONSERVED SEQUENCE; DIMERIZATION; GLUTAMINE; HUMANS; HYDROPHOBICITY; MOLECULAR WEIGHT; MUTATION; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 33644858451     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052051k     Document Type: Article

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