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Amphipathic solvation of indole: implications for the role of tryptophan in membrane proteins

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Johnston, Andrew J
Zhang, Yapei
Busch, Sebastian
Pardo Soto, Luis CarlosMés informacióMés informacióMés informació
Imberti, Silvia
McLain, Sylvia E.
Document typeArticle
Defense date2015-05-14
Rights accessOpen Access
Attribution-NonCommercial-NoDerivs 3.0 Spain
Except where otherwise noted, content on this work is licensed under a Creative Commons license : Attribution-NonCommercial-NoDerivs 3.0 Spain
Abstract
The microscopic structure of the tryptophan side chain, indole, in an amphiphilic environment has been investigated using a combination of neutron diffraction measurements and simulations in solution. The results show that indole is preferentially solvated by hydrogen bonding interactions between water and alcohol -OH groups rather than the interaction being dominated by indole-methyl interactions. This has implications for understanding how tryptophan interacts with the amphipathic membrane environment to anchor proteins into membranes, where the results here suggest that the benzene ring of tryptophan interacts directly with the interfacial water at the membrane surface rather than being buried into the hydrophobic regions of the membrane bilayer.
CitationJohnston, A., Zhang, Y., Busch, S., Pardo, L., Imberti, S., McLain, S. Amphipathic solvation of indole: implications for the role of tryptophan in membrane proteins. "Journal of physical chemistry B", 14 Maig 2015, vol. 119, núm. 19, p. 5979-5987. 
URIhttp://hdl.handle.net/2117/79468
DOI10.1021/acs.jpcb.5b02476
ISSN1520-6106
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  • Departament de Física - Articles de revista [1.857]
  • GCM - Grup de Caracterització de Materials - Articles de revista [332]
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