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Comparison of the structures and stabilities of coiled-coil proteins containing hexafluoroleucine and t-butylalanine provides insight into the stabilizing effects of highly fluorinated amino acid side-chains

Highly fluorinated analogs of hydrophobic amino acids are well known to increase the stability of proteins toward thermal unfolding and chemical denaturation, but there is very little data on the structural consequences of fluorination. We have determined the structures and folding energies of three...

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Main Authors: Buer, Benjamin C, Meagher, Jennifer L, Stuckey, Jeanne A, Marsh, E Neil G
格式: Artigo
語言:Inglês
出版: Wiley Subscription Services, Inc., A Wiley Company 2012
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC3527707/
https://ncbi.nlm.nih.gov/pubmed/22930450
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2150
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