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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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Bibliografiske detaljer
Udgivet i:Cell Stress Chaperones
Main Authors: Chalova, Anna S., Sudnitsyna, Maria V., Semenyuk, Pavel I., Orlov, Victor N., Gusev, Nikolai B.
Format: Artigo
Sprog:Inglês
Udgivet: Springer Netherlands 2014
Fag:
Online adgang: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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