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pro vyhledávání: '"Sarah E. D. Nelson"'
Autor:
Sarah E. D. Nelson, Daniel K. Weber, Robyn T. Rebbeck, Razvan L. Cornea, Gianluigi Veglia, David D. Thomas
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Abstract We have used NMR and circular dichroism spectroscopy to investigate the structural and dynamic effects of oxidation on calmodulin (CaM), using peroxide and the Met to Gln oximimetic mutations. CaM is a Ca2+-sensitive regulatory protein that
Externí odkaz:
https://doaj.org/article/36f3e28887f142c5b2edc2e310a92fe1
Publikováno v:
The journal of physical chemistry. B. 121(17)
Proteins exist in ensembles of conformational states that interconvert on various motional time scales. High-energy states of proteins, often referred to as conformationally excited states, are sparsely populated and have been found to play an essent