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The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts

The peptide backbones of disordered proteins are routinely characterized by NMR with respect to transient structure and dynamics. Little experimental information is, however, available about the side chain conformations and how structure in the backbone affects the side chains. Methyl chemical shift...

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Bibliografske podrobnosti
Main Authors: Kjaergaard, Magnus, Iešmantavičius, Vytautas, Poulsen, Flemming M
Format: Artigo
Jezik:Inglês
Izdano: Wiley Subscription Services, Inc., A Wiley Company 2011
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC3302646/
https://ncbi.nlm.nih.gov/pubmed/21898648
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.726
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