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Modeling transient collapsed states of an unfolded protein to provide insights into early folding events

The primary driving force for protein folding is the sequestration of hydrophobic side chains from solvent water, but the means whereby the amino acid sequence directs the folding process to form the correct final folded state is not well understood. Measurements of NMR line broadening in spin-label...

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Bibliografski detalji
Glavni autori: Felitsky, Daniel J., Lietzow, Michael A., Dyson, H. Jane, Wright, Peter E.
Format: Artigo
Jezik:Inglês
Izdano: National Academy of Sciences 2008
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2359776/
https://ncbi.nlm.nih.gov/pubmed/18434548
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0710641105
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