Critical role of tryptophanyl residues in the conformational stability of goose δ-crystallin

Experimental Eye Research

Volumn 83, Issue 3, 2006, Pages 658-666

  Lee, Hwei Jen ^a   Lai, Young Hsang ^a   Huang, Yu Ting ^a   Huang, Chih Wei ^a   Chen, Yu Hou ^b   Chang, Gu Gang ^b  

^a NATIONAL DEFENSE MEDICAL CENTER   (Taiwan)

^b NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

argininosuccinate lyase; conformational stability; goose crystallin; protein unfolding; subunit assembly; tryptophan residue replacement

Indexed keywords

ALANINE; AMINO ACID; DELTA CRYSTALLIN; GUANIDINE; PHENYLALANINE; TRYPTOPHAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; FLUORESCENCE; GOOSE; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SEDIMENTATION RATE; TEMPERATURE; THERMOSTABILITY; WILD TYPE;

ANIMALS; ARGININOSUCCINATE LYASE; BASE SEQUENCE; DELTA-CRYSTALLINS; GEESE; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 33745236036     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2006.03.001     Document Type: Article

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