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

Temperature-induced conformational changes of reduced and oxidized HspB1 crosslinked by disulfide bond between single Cys137 of neighboring monomers were analyzed by means of different techniques. Heating of reduced HspB1 was accompanied by irreversible changes of Trp fluorescence, whereas oxidized...

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Detalles Bibliográficos
Publicado en:Cell Stress Chaperones
Main Authors: Chalova, Anna S., Sudnitsyna, Maria V., Semenyuk, Pavel I., Orlov, Victor N., Gusev, Nikolai B.
Formato: Artigo
Idioma:Inglês
Publicado: Springer Netherlands 2014
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC4389837/
https://ncbi.nlm.nih.gov/pubmed/24898092
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12192-014-0520-9
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