Trehalose favors a cutinase compact intermediate off-folding pathway

Biochemistry

Volumn 42, Issue 24, 2003, Pages 7611-7617

  Melo, Eduardo P ^a,b   Chen, Lu Yang ^b   Cabral, Joaquim M S ^b   Fojan, Peter ^c   Petersen, Steffen B ^c   Otzen, Daniel E ^c  

^a UNIVERSITY OF ALGARVE   (Portugal)

^b INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^c AALBORG UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

FREE ENERGY; MATHEMATICAL MODELS; RATE CONSTANTS; SOLVENTS;

TREHALOSE CONCENTRATION;

ENZYMES;

CUTINASE; GUANIDINE; SOLVENT; TREHALOSE;

ARTICLE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DECELERATION; ENERGY; ENZYME ACTIVITY; KINETICS; LIPOLYSIS; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY;

CARBOXYLIC ESTER HYDROLASES; CLONING, MOLECULAR; ENZYME STABILITY; FUSARIUM; GUANIDINES; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SOLVENTS; THERMODYNAMICS; TREHALOSE;

EID: 0038070096     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034267x     Document Type: Article

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