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

Author
Johnston, A.; Zhang, Y.; Busch, S.; Pardo, L.; Imberti, S.; McLain, S.
Type of activity
Journal article
Journal
Journal of physical chemistry B
Date of publication
2015-05-14
Volume
119
Number
19
First page
5979
Last page
5987
DOI
https://doi.org/10.1021/acs.jpcb.5b02476 Open in new window
Project funding
Dinámica en sólidos desordenados
Repository
http://hdl.handle.net/2117/79468 Open in new window
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 env...
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.
Keywords
Aqueous-solution, Aromatic rings, Gramicidin channel, Hydrogen-bond acceptors, Lipid bilayers, Molecular-dynamics, Neutron-diffraction, Peptides, Pi interactions, Water
Group of research
CRnE - Barcelona Research Center in Multiscale Science and Engineering
GCM - Group of Characterization of Materials

Participants

  • Johnston, Andrew J  (author)
  • Zhang, Yapei  (author)
  • Busch, Sebastian  (author)
  • Pardo Soto, Luis Carlos  (author)
  • Imberti, Silvia  (author)
  • McLain, Sylvia E.  (author)

Attachments