Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins

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 wa...

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Veröffentlicht in:	The journal of physical chemistry. B 2015-05, Vol.119 (19), p.5979-5987
Hauptverfasser:	Johnston, Andrew J, Zhang, Yapei (Rosie), Busch, Sebastian, Pardo, Luis Carlos, Imberti, Silvia, McLain, Sylvia E
Format:	Artikel
Sprache:	eng
Schlagworte:	Aqueous-solution Aromatic rings Computer Simulation Enginyeria dels materials Enginyeria química Gramicidin channel Hydrogen - chemistry Hydrogen Bonding Hydrogen-bond acceptors Hydrophobic and Hydrophilic Interactions Indoles Indoles - chemistry Lipid bilayers Membrane Proteins - chemistry Membranes Membranes (Biologia) Membranes (Biology) Methanol - chemistry Models, Chemical Molecular-dynamics Neutron Diffraction Oxygen - chemistry Peptides Physical chemistry Pi interactions Proteins Proteïnes Química física Simulation Solvents - chemistry Tryptophan Tryptophan - chemistry Water Water - chemistry Àrees temàtiques de la UPC
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