Probing molecular motion by NMR
Recently developed solution NMR methods for measuring 2H, 13C, and 15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical i...
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| Veröffentlicht in: | Current opinion in structural biology 1997-10, Vol.7 (5), p.732-737 |
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| container_end_page | 737 |
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| container_issue | 5 |
| container_start_page | 732 |
| container_title | Current opinion in structural biology |
| container_volume | 7 |
| creator | Palmer, Arthur G |
| description | Recently developed solution NMR methods for measuring
2H,
13C, and
15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins. |
| doi_str_mv | 10.1016/S0959-440X(97)80085-1 |
| format | Article |
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2H,
13C, and
15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins.</description><identifier>ISSN: 0959-440X</identifier><identifier>EISSN: 1879-033X</identifier><identifier>DOI: 10.1016/S0959-440X(97)80085-1</identifier><identifier>PMID: 9345634</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Carbon Isotopes ; Catalysis ; Deuterium ; Diffusion ; Ligands ; Magnetic Resonance Spectroscopy - methods ; Membrane Proteins - chemistry ; Nitrogen Isotopes ; Protein Conformation ; Proteins - chemistry ; Proteins - metabolism</subject><ispartof>Current opinion in structural biology, 1997-10, Vol.7 (5), p.732-737</ispartof><rights>1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c407t-1076de5ba748be46fd55d23935da554c01b727dfde19b70bf6c04c36c06f779c3</citedby><cites>FETCH-LOGICAL-c407t-1076de5ba748be46fd55d23935da554c01b727dfde19b70bf6c04c36c06f779c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0959440X97800851$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9345634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Palmer, Arthur G</creatorcontrib><title>Probing molecular motion by NMR</title><title>Current opinion in structural biology</title><addtitle>Curr Opin Struct Biol</addtitle><description>Recently developed solution NMR methods for measuring
2H,
13C, and
15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins.</description><subject>Carbon Isotopes</subject><subject>Catalysis</subject><subject>Deuterium</subject><subject>Diffusion</subject><subject>Ligands</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Membrane Proteins - chemistry</subject><subject>Nitrogen Isotopes</subject><subject>Protein Conformation</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><issn>0959-440X</issn><issn>1879-033X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUMlKA0EUbESJMfoJwZxED6Ov09v0SSS4QVxwgdya6WWkZZbYPSPk751kQq5e3ntQVa-oQmiM4RID5lfvIJlMKIXFuRQXKUDKEryHhjgVMgFCFvtouKMcoqMYvwGAY5oO0EASyjihQ3T6Gmrtq69JWRfOtEUWuqvxdTXRq8nz09sxOsizIrqT7R6hz7vbj9lDMn-5f5zdzBNDQTQJBsGtYzoTNNWO8twyZqdEEmYzxqgBrMVU2Nw6LLUAnXMD1JBu8lwIacgInfV_l6H-aV1sVOmjcUWRVa5uoxKScDKlaUdkPdGEOsbgcrUMvszCSmFQ62LUphi1Tq2kUJtiFO50461Bq0tnd6ptEx1-3eOuS_nrXVDReFcZZ31wplG29v84_AEttnFq</recordid><startdate>19971001</startdate><enddate>19971001</enddate><creator>Palmer, Arthur G</creator><general>Elsevier Ltd</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>19971001</creationdate><title>Probing molecular motion by NMR</title><author>Palmer, Arthur G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-1076de5ba748be46fd55d23935da554c01b727dfde19b70bf6c04c36c06f779c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Carbon Isotopes</topic><topic>Catalysis</topic><topic>Deuterium</topic><topic>Diffusion</topic><topic>Ligands</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Membrane Proteins - chemistry</topic><topic>Nitrogen Isotopes</topic><topic>Protein Conformation</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Palmer, Arthur G</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>Current opinion in structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Palmer, Arthur G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Probing molecular motion by NMR</atitle><jtitle>Current opinion in structural biology</jtitle><addtitle>Curr Opin Struct Biol</addtitle><date>1997-10-01</date><risdate>1997</risdate><volume>7</volume><issue>5</issue><spage>732</spage><epage>737</epage><pages>732-737</pages><issn>0959-440X</issn><eissn>1879-033X</eissn><abstract>Recently developed solution NMR methods for measuring
2H,
13C, and
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| fulltext | fulltext |
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| ispartof | Current opinion in structural biology, 1997-10, Vol.7 (5), p.732-737 |
| issn | 0959-440X 1879-033X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79363248 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Carbon Isotopes Catalysis Deuterium Diffusion Ligands Magnetic Resonance Spectroscopy - methods Membrane Proteins - chemistry Nitrogen Isotopes Protein Conformation Proteins - chemistry Proteins - metabolism |
| title | Probing molecular motion by NMR |
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