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Amphipathic solvation of indole: implications for the role of tryptophan in membrane proteins
dc.contributor.author | Johnston, Andrew J |
dc.contributor.author | Zhang, Yapei |
dc.contributor.author | Busch, Sebastian |
dc.contributor.author | Pardo Soto, Luis Carlos |
dc.contributor.author | Imberti, Silvia |
dc.contributor.author | McLain, Sylvia E. |
dc.contributor.other | Universitat Politècnica de Catalunya. Departament de Física |
dc.date.accessioned | 2015-11-19T10:19:31Z |
dc.date.available | 2016-05-04T00:32:05Z |
dc.date.issued | 2015-05-14 |
dc.identifier.citation | Johnston, 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. |
dc.identifier.issn | 1520-6106 |
dc.identifier.uri | http://hdl.handle.net/2117/79468 |
dc.description.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. |
dc.format.extent | 9 p. |
dc.language.iso | eng |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ |
dc.subject | Àrees temàtiques de la UPC::Enginyeria química::Química física |
dc.subject | Àrees temàtiques de la UPC::Enginyeria dels materials |
dc.subject.lcsh | Proteins |
dc.subject.lcsh | Membranes (Biology) |
dc.subject.other | Hydrogen-bond acceptors |
dc.subject.other | Gramicidin channel |
dc.subject.other | Neutron-diffraction |
dc.subject.other | Molecular-dynamics |
dc.subject.other | Aqueous-solution |
dc.subject.other | Pi interactions |
dc.subject.other | Lipid bilayers |
dc.subject.other | Aromatic rings |
dc.subject.other | Water |
dc.subject.other | Peptides |
dc.title | Amphipathic solvation of indole: implications for the role of tryptophan in membrane proteins |
dc.type | Article |
dc.subject.lemac | Proteïnes |
dc.subject.lemac | Membranes (Biologia) |
dc.contributor.group | Universitat Politècnica de Catalunya. GCM - Grup de Caracterització de Materials |
dc.identifier.doi | 10.1021/acs.jpcb.5b02476 |
dc.rights.access | Open Access |
local.identifier.drac | 16387173 |
dc.description.version | Postprint (author's final draft) |
local.citation.author | Johnston, A.; Zhang, Y.; Busch, S.; Pardo, L.; Imberti, S.; McLain, S. |
local.citation.publicationName | Journal of physical chemistry B |
local.citation.volume | 119 |
local.citation.number | 19 |
local.citation.startingPage | 5979 |
local.citation.endingPage | 5987 |
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