β-strand interactions at the domain interface critical for the stability of human lens γD-crystallin

Protein Science

Volumn 19, Issue 1, 2010, Pages 131-140

  Das, Payel ^a   King, Jonathan A ^b   Zhou, Ruhong ^a,c  

^a IBM T J WATSON RESEARCH CENTER   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c Howard Hughes Medical Institute   (United States)

Author keywords

Beta sheet protein folding; Eye cataracts; Molecular dynamics; Non native interaction

Indexed keywords

ARGININE; GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; GLUTAMIC ACID; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATARACT; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

ARGININE; GAMMA-CRYSTALLINS; GLUTAMIC ACID; HUMANS; MOLECULAR DYNAMICS SIMULATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 75149175314     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.296     Document Type: Article

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