Using buried water molecules to explore the energy landscape of proteins
Buried water molecules constitute a highly conserved, integral part of nearly all known protein structures. Such water molecules exchange with external solvent as a result of protein conformational fluctuations. We report here the results of water 17 O and 2 H magnetic relaxation dispersion measurem...
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| Veröffentlicht in: | Nature Structural Biology 1996-06, Vol.3 (6), p.505-509 |
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| container_issue | 6 |
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| container_title | Nature Structural Biology |
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| creator | Denisov, Vladimir P. Peters, Jörg Hörlein, Hans Dietrich Halle, Bertil |
| description | Buried water molecules constitute a highly conserved, integral part of nearly all known protein structures. Such water molecules exchange with external solvent as a result of protein conformational fluctuations. We report here the results of water
17
O and
2
H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4–80 °C. These data lead to the first determination of the exchange rate of a water molecule buried in a protein. The strong temperature dependence of this rate is ascribed to large-scale conformational fluctuations in an energy landscape with a statistical ruggedness of ∼10 kJ mol
−1
. |
| doi_str_mv | 10.1038/nsb0696-505 |
| format | Article |
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17
O and
2
H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4–80 °C. These data lead to the first determination of the exchange rate of a water molecule buried in a protein. The strong temperature dependence of this rate is ascribed to large-scale conformational fluctuations in an energy landscape with a statistical ruggedness of ∼10 kJ mol
−1
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17
O and
2
H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4–80 °C. These data lead to the first determination of the exchange rate of a water molecule buried in a protein. The strong temperature dependence of this rate is ascribed to large-scale conformational fluctuations in an energy landscape with a statistical ruggedness of ∼10 kJ mol
−1
.</description><subject>Aprotinin - chemistry</subject><subject>Aprotinin - genetics</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Energy Transfer</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Temperature</subject><subject>Water - chemistry</subject><subject>Water - metabolism</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkDtPwzAURi0EKqUwMSN5YoGAH_FrRBUvqRILna0kvimpkrjYiaD_HqNGTEy-0nf0Xd-D0CUld5Rwfd_HkkgjM0HEEZpTkYvMGC2O00wUyzSX-hSdxbglhAmh-AzNtMyl4GKOXtax6Te4HEMDDn8VAwTc-RaqsYWIB4_he9f6AHj4AAw9hM0et0XvYlXsAPsa74IfoOnjOTqpizbCxfQu0Prp8X35kq3enl-XD6us4loNWQ2CG1YJbbQuHCdKSpCkBCqBMkedYBQ4dyQnUDJWSZ07A65WCripc8X4Al0fetPizxHiYLsmVtCmT4Efo1WaSGVynsCbA1gFH2OA2u5C0xVhbymxv97s5M0mb4m-mmrHsgP3x06iUn57yGNK-g0Eu_Vj6NOl_9b9ABPqd0o</recordid><startdate>19960601</startdate><enddate>19960601</enddate><creator>Denisov, Vladimir P.</creator><creator>Peters, Jörg</creator><creator>Hörlein, Hans Dietrich</creator><creator>Halle, Bertil</creator><general>Nature Publishing Group US</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></search><sort><creationdate>19960601</creationdate><title>Using buried water molecules to explore the energy landscape of proteins</title><author>Denisov, Vladimir P. ; Peters, Jörg ; Hörlein, Hans Dietrich ; Halle, Bertil</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c387t-fe5392c58988ad30766e60be16e12d1d521e33d040eb22c684d9edf77e39f4723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Aprotinin - chemistry</topic><topic>Aprotinin - genetics</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Energy Transfer</topic><topic>Life Sciences</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Membrane Biology</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>Protein Structure</topic><topic>Temperature</topic><topic>Water - chemistry</topic><topic>Water - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Denisov, Vladimir P.</creatorcontrib><creatorcontrib>Peters, Jörg</creatorcontrib><creatorcontrib>Hörlein, Hans Dietrich</creatorcontrib><creatorcontrib>Halle, Bertil</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><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Denisov, Vladimir P.</au><au>Peters, Jörg</au><au>Hörlein, Hans Dietrich</au><au>Halle, Bertil</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Using buried water molecules to explore the energy landscape of proteins</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>1996-06-01</date><risdate>1996</risdate><volume>3</volume><issue>6</issue><spage>505</spage><epage>509</epage><pages>505-509</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Buried water molecules constitute a highly conserved, integral part of nearly all known protein structures. Such water molecules exchange with external solvent as a result of protein conformational fluctuations. We report here the results of water
17
O and
2
H magnetic relaxation dispersion measurements on wild-type and mutant bovine pancreatic trypsin inhibitor in aqueous solution at 4–80 °C. These data lead to the first determination of the exchange rate of a water molecule buried in a protein. The strong temperature dependence of this rate is ascribed to large-scale conformational fluctuations in an energy landscape with a statistical ruggedness of ∼10 kJ mol
−1
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| ispartof | Nature Structural Biology, 1996-06, Vol.3 (6), p.505-509 |
| issn | 1072-8368 1545-9993 1545-9985 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals; Nature Journals Online |
| subjects | Aprotinin - chemistry Aprotinin - genetics Biochemistry Biological Microscopy Biomedical and Life Sciences Energy Transfer Life Sciences Magnetic Resonance Spectroscopy - methods Membrane Biology Models, Molecular Mutation Protein Conformation Protein Structure Temperature Water - chemistry Water - metabolism |
| title | Using buried water molecules to explore the energy landscape of proteins |
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