Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures

Protein Engineering, Design and Selection

Volumn 23, Issue 5, 2010, Pages 393-402

  Kanzaki, Taro ^a   Ushioku, Shuzo ^a   Nakagawa, Ayumi ^a   Oka, Toshihiko ^b   Takahashi, Kazunobu ^c,d   Nakamura, Takashi ^c   Kuwajima, Kunihiro ^c,e   Yamagishi, Akihiko ^f   Yohda, Masafumi ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b SHIZUOKA UNIVERSITY   (Japan)

^c OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

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

Author keywords

Cold adaptation; Group II chaperonin; Hyperthermophilic archaeon; Protein folding; Small angle X ray scattering

Indexed keywords

AMINO ACID SEQUENCE; ANALYTICAL METHOD; ARCHAEA; CHAPERONIN; CONFORMATIONAL CHANGE; EUKARYOTIC CYTOSOL; GROUP II CHAPERONIN; GROUP II CHAPERONINS; HIGH STABILITY; HOMO-OLIGOMERS; HYPERTHERMOPHILIC; HYPERTHERMOPHILIC ARCHAEON; LOW TEMPERATURES; MESOPHILIC; MODERATE TEMPERATURE; OPTIMAL TEMPERATURE; REACTION MECHANISM; SINGLE MUTANT; SINGLE MUTATION; SMALL ANGLE X-RAY SCATTERING; THERMOPHILICITY;

AMINO ACIDS; ORGANIC ACIDS; PROTEIN FOLDING; X RAY SCATTERING;

SCATTERING;

ADENOSINE TRIPHOSPHATE; ALPHA CHAPERONIN; ARGININE; CHAPERONIN; LYSINE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; COLD ACCLIMATIZATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; LOW TEMPERATURE; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMOCOCCUS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BASE SEQUENCE; DNA PRIMERS; GROUP II CHAPERONINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION, MISSENSE; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; TEMPERATURE; THERMOCOCCUS;

ARCHAEA; EUKARYOTA; THERMOCOCCUS SP.;

EID: 77951145446     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq010     Document Type: Article

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