Eye lens βB2-crystallin: Circular permutation does not influence the oligomerization state but enhances the conformational stability

Journal of Molecular Biology

Volumn 280, Issue 4, 1998, Pages 721-729

  Wieligmann, Karin ^a   Norledge, Brian ^b   Jaenicke, Rainer ^a   Mayr, Eva Maria ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b Birkbeck College   (United Kingdom)

Author keywords

Circular permutation; Crystallins; Domain association; Oligomerization; Protein stability

Indexed keywords

CRYSTALLIN; LENS PROTEIN; UREA; BETA CRYSTALLIN; BETA CRYSTALLIN B2; BETA-CRYSTALLIN B2; DRUG DERIVATIVE; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE; GENETIC ENGINEERING; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; RAT; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; ESCHERICHIA COLI; EYE; GENETICS; LENS; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

VERTEBRATA;

AMINO ACID SEQUENCE; ANIMALS; BETA-CRYSTALLIN B CHAIN; CRYSTALLINS; ESCHERICHIA COLI; EYE; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0032562996     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1887     Document Type: Article

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