Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 2, 2013, Pages 621-628

  Choi, Dongwook ^a,b   Ryu, Kyoung Seok ^b   Park, Chankyu ^a  

^a Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^b Korea Basic Science Institute (KBSI)   (South Korea)

Author keywords

Chaperone; Conformational change; Glyoxalase; Hsp31; Keywords; Oligomerization

Indexed keywords

CHAPERONE; DIMER; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 31; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE; HYDROPHOBICITY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE;

AMINO ACID SEQUENCE; ESCHERICHIA COLI K12; ESCHERICHIA COLI PROTEINS; HOT TEMPERATURE; HSP30 HEAT-SHOCK PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION;

ESCHERICHIA COLI;

EID: 84872168612     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.11.006     Document Type: Article

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