Roles for the two N-terminal (δ/α) modules in the folding of a (δ/α) 8-barrel protein as studied by fragmentation analysis

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 1, 2011, Pages 221-231

  Akanuma, Satoshi ^a   Yamagishi, Akihiko ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

( ) 8 barrel; Folding intermediate; Folding scaffold; Fragmentation; Nucleation site; Stability

Indexed keywords

BACTERIAL PROTEIN; BETA ALPHA 8 BARREL PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE; FRAGMENTATION REACTION; GEL FILTRATION; HYDROPHOBICITY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEPLETION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

ALDOSE-KETOSE ISOMERASES; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; STRUCTURAL HOMOLOGY, PROTEIN; UREA;

ESCHERICHIA COLI;

EID: 78649782932     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22874     Document Type: Article

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