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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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Autors principals: Felitsky, Daniel J., Lietzow, Michael A., Dyson, H. Jane, Wright, Peter E.
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2008
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Accés en línia: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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