Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1

Cell Stress and Chaperones

Volumn 19, Issue 6, 2014, Pages 963-972

  Chalova, Anna S ^a   Sudnitsyna, Maria V ^a   Semenyuk, Pavel I ^a   Orlov, Victor N ^a   Gusev, Nikolai B ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Disulfide crosslinking; Oligomeric structure; Small heat shock proteins; Thermal stability

Indexed keywords

CYSTEINE; DISULFIDE; HEAT SHOCK PROTEIN 27; HSPB1 PROTEIN, HUMAN; RECOMBINANT PROTEIN;

CHEMISTRY; FLUOROMETRY; HEAT; HUMAN; LIGHT; METABOLISM; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; RADIATION SCATTERING; STRUCTURE ACTIVITY RELATION;

CYSTEINE; DISULFIDES; FLUOROMETRY; HOT TEMPERATURE; HSP27 HEAT-SHOCK PROTEINS; HUMANS; LIGHT; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; RECOMBINANT PROTEINS; SCATTERING, RADIATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84939887279     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-014-0520-9     Document Type: Article

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