Oxidation of buried cysteines is slow and an insignificant factor in the structural destabilization of staphylococcal nuclease caused by H 2O2 exposure

Amino Acids

Volumn 27, Issue 2, 2004, Pages 175-181

  Kim, Y H ^a   Stites, W E ^a  

^a UNIVERSITY OF ARKANSAS   (United States)

Author keywords

Enzyme activity; Rate; Redox; Regulation; Solvent accessibility

Indexed keywords

CYSTEINE; METHIONINE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; FEASIBILITY STUDY; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN STRUCTURE;

BINDING SITES; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME STABILITY; HYDROGEN PEROXIDE; METHIONINE; MICROCOCCAL NUCLEASE; OXIDATION-REDUCTION; OXYGEN; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN S; SOLVENTS; THERMODYNAMICS;

EID: 8644242927     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-004-0110-8     Document Type: Article

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