Thermal unfolding of chitosanase from Streptomyces sp. N174: Role of tryptophan residues in the protein structure stabilization

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1429, Issue 2, 1999, Pages 365-376

  Honda, Yuji ^a   Fukamizo, Tamo ^a   Okajima, Toshihide ^a   Goto, Sachio ^a   Boucher, Isabelle ^b   Brzezinski, Ryszard ^b  

^a Kinki University   (Japan)

^b UNIVERSITÉ DE SHERBROOKE   (Canada)

Author keywords

Chitosanase; Molten globule; Site directed mutagenesis; Thermal unfolding; Tryptophan residue

Indexed keywords

CHITOSANASE; MUTANT PROTEIN; TRYPTOPHAN;

ARTICLE; CIRCULAR DICHROISM; ENZYME KINETICS; ENZYME PURIFICATION; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STREPTOMYCES LIVIDANS;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; GLYCOSIDE HYDROLASES; MUTATION; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; STREPTOMYCES; TRYPTOPHAN; X-RAY DIFFRACTION;

EID: 0032928871     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00243-X     Document Type: Article

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