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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.

Original publication




Journal article


J Phys Chem B

Publication Date





5979 - 5987


Computer Simulation, Hydrogen, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Indoles, Membrane Proteins, Methanol, Models, Chemical, Neutron Diffraction, Oxygen, Solvents, Tryptophan, Water