Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s12551-021-00916-4.pdf
Reference108 articles.
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2. Andrałojć W, Luchinat C, Parigi G, Ravera E (2014) Exploring regions of conformational space occupied by two-domain proteins. J Phys Chem B 118:10576–10587. https://doi.org/10.1021/JP504820W
3. Andrałojć W, Ravera E, Salmon L et al (2016) Inter-helical conformational preferences of HIV-1 TAR-RNA from maximum occurrence analysis of NMR data and molecular dynamics simulations. Phys Chem Chem Phys 18:5743–5752. https://doi.org/10.1039/c5cp03993b
4. Anthis NJ, Doucleff M, Clore GM (2011) Transient, sparsely populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: interplay of conformational selection and induced fit. J Am Chem Soc 133:18966–18974. https://doi.org/10.1021/JA2082813
5. Banci L, Bertini I, Bren KL et al (1996) The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example. J Biol Inorg Chem 1:117–126. https://doi.org/10.1007/s007750050030
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