"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Transition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding,...
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| Format: | Article |
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2015
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| Series: | CHEMISTRY-A EUROPEAN JOURNAL
21 No. 13 |
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| mtmt: | 2871042 |
| Online Access: | https://publikacio.ppke.hu/1469 |