Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose

Journal of Biological Chemistry

Volumn 278, Issue 29, 2003, Pages 26458-26465

  Kaushik, Jai K ^a   Bhat, Rajiv ^b  

^a NATIONAL DAIRY RESEARCH INSTITUTE   (India)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GIBBS FREE ENERGY; PH EFFECTS; SOLUTIONS;

DENATURATION;

BIOCHEMISTRY;

CARBOHYDRATE; POLYOL; POLYPEPTIDE; RIBONUCLEASE; SOLVENT; STABILIZING AGENT; TREHALOSE; WATER;

AQUEOUS SOLUTION; ARTICLE; CONCENTRATION RESPONSE; CORRELATION ANALYSIS; ENZYME ACTIVITY; HIGH TEMPERATURE; LINKAGE ANALYSIS; PH; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FUNCTION; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ALPHA-AMYLASE; ANIMALS; CATTLE; CHEMISTRY, PHYSICAL; CHYMOTRYPSINOGEN; CYTOCHROME C GROUP; DRUG STABILITY; ENZYME STABILITY; EXCIPIENTS; KINETICS; MURAMIDASE; PLANT PROTEINS; PROTEIN DENATURATION; PROTEINS; RIBONUCLEASE, PANCREATIC; SOLUTIONS; SURFACE TENSION; TEMPERATURE; THERMODYNAMICS; TREHALOSE; TRYPSIN INHIBITORS;

EID: 0038374325     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M300815200     Document Type: Article

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