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 |
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| container_end_page | 5987 |
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| container_issue | 19 |
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| container_title | The journal of physical chemistry. B |
| container_volume | 119 |
| creator | Johnston, Andrew J Zhang, Yapei (Rosie) Busch, Sebastian Pardo, Luis Carlos Imberti, Silvia McLain, Sylvia E |
| description | 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. |
| doi_str_mv | 10.1021/acs.jpcb.5b02476 |
| format | Article |
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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. 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B</title><addtitle>J. Phys. Chem. B</addtitle><description>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.</description><subject>Aqueous-solution</subject><subject>Aromatic rings</subject><subject>Computer Simulation</subject><subject>Enginyeria dels materials</subject><subject>Enginyeria química</subject><subject>Gramicidin channel</subject><subject>Hydrogen - chemistry</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen-bond acceptors</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Indoles</subject><subject>Indoles - chemistry</subject><subject>Lipid bilayers</subject><subject>Membrane Proteins - chemistry</subject><subject>Membranes</subject><subject>Membranes (Biologia)</subject><subject>Membranes (Biology)</subject><subject>Methanol - chemistry</subject><subject>Models, Chemical</subject><subject>Molecular-dynamics</subject><subject>Neutron Diffraction</subject><subject>Oxygen - chemistry</subject><subject>Peptides</subject><subject>Physical chemistry</subject><subject>Pi interactions</subject><subject>Proteins</subject><subject>Proteïnes</subject><subject>Química física</subject><subject>Simulation</subject><subject>Solvents - chemistry</subject><subject>Tryptophan</subject><subject>Tryptophan - chemistry</subject><subject>Water</subject><subject>Water - chemistry</subject><subject>Àrees temàtiques de la UPC</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>XX2</sourceid><recordid>eNqFUU1v1DAQtSpQPxbuPSEfObCLv5NwqyqgKxWBoByRZXvHWldJHOykUv89TjdtT6iHkWc87z2P5yF0TsmGEkY_Gpc3t4OzG2kJE5U6QqdUMrIuUb1ackWJOkFnOd8SwiSr1TE6YbJueCXoKfpz0Q37MJhxHxz-Fds7M4bY4-jxtt_FFj7hbTe0wT1cZ-xjwuMe8M_SmkE36X4Y47A3PQ49_gadTaYH_CPFEUKf36DX3rQZ3i7nCv3-8vnm8mp9_f3r9vLiem2E5ONauAaIgsrzxgAIaZlUoBSvPKmbhnuyU0I4yY20wKmXyljBLN0xLqQ31PIVogddlyenEzhIZWIdTXgu5ihrYZrzhpVnV-j9gTOk-HeCPOouZAdtWz4Qp6xppRiRNRfsZaiqKVOM8lmVLJOkmHMCr4cUOpPuNSV69kwXz_TsmV48K5R3i_pkO9g9ER5NKoAPB8ADNU6pL7v8v94_MGWiAA</recordid><startdate>20150514</startdate><enddate>20150514</enddate><creator>Johnston, Andrew J</creator><creator>Zhang, Yapei (Rosie)</creator><creator>Busch, Sebastian</creator><creator>Pardo, Luis Carlos</creator><creator>Imberti, Silvia</creator><creator>McLain, Sylvia E</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>XX2</scope></search><sort><creationdate>20150514</creationdate><title>Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins</title><author>Johnston, Andrew J ; Zhang, Yapei (Rosie) ; Busch, Sebastian ; Pardo, Luis Carlos ; Imberti, Silvia ; McLain, Sylvia E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a453t-4c9e06e7f39aee45b256e6637f08993f0d644c53a5be31f56ab42b1d2345fa1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Aqueous-solution</topic><topic>Aromatic rings</topic><topic>Computer Simulation</topic><topic>Enginyeria dels materials</topic><topic>Enginyeria química</topic><topic>Gramicidin channel</topic><topic>Hydrogen - chemistry</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen-bond acceptors</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Indoles</topic><topic>Indoles - chemistry</topic><topic>Lipid bilayers</topic><topic>Membrane Proteins - chemistry</topic><topic>Membranes</topic><topic>Membranes (Biologia)</topic><topic>Membranes (Biology)</topic><topic>Methanol - chemistry</topic><topic>Models, Chemical</topic><topic>Molecular-dynamics</topic><topic>Neutron Diffraction</topic><topic>Oxygen - chemistry</topic><topic>Peptides</topic><topic>Physical chemistry</topic><topic>Pi interactions</topic><topic>Proteins</topic><topic>Proteïnes</topic><topic>Química física</topic><topic>Simulation</topic><topic>Solvents - chemistry</topic><topic>Tryptophan</topic><topic>Tryptophan - chemistry</topic><topic>Water</topic><topic>Water - chemistry</topic><topic>Àrees temàtiques de la UPC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnston, Andrew J</creatorcontrib><creatorcontrib>Zhang, Yapei (Rosie)</creatorcontrib><creatorcontrib>Busch, Sebastian</creatorcontrib><creatorcontrib>Pardo, Luis Carlos</creatorcontrib><creatorcontrib>Imberti, Silvia</creatorcontrib><creatorcontrib>McLain, Sylvia E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Recercat</collection><jtitle>The journal of physical chemistry. 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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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>25893741</pmid><doi>10.1021/acs.jpcb.5b02476</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 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 |
| title | Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins |
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