Functional dynamics of proteins revealed by solution NMR
► Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ► Recent progresses in a variety of NMR techniques are reviewed. ► Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ► NMR applications to functionally relevant protein dynami...
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Veröffentlicht in: | Current opinion in structural biology 2012-10, Vol.22 (5), p.660-669 |
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creator | Osawa, Masanori Takeuchi, Koh Ueda, Takumi Nishida, Noritaka Shimada, Ichio |
description | ► Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ► Recent progresses in a variety of NMR techniques are reviewed. ► Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ► NMR applications to functionally relevant protein dynamics are also introduced.
Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been ‘invisible’ with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics. |
doi_str_mv | 10.1016/j.sbi.2012.08.007 |
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Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been ‘invisible’ with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics.</description><identifier>ISSN: 0959-440X</identifier><identifier>EISSN: 1879-033X</identifier><identifier>DOI: 10.1016/j.sbi.2012.08.007</identifier><identifier>PMID: 23000032</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Humans ; Nuclear Magnetic Resonance, Biomolecular - methods ; Proteins - chemistry ; Proteins - metabolism ; Solutions</subject><ispartof>Current opinion in structural biology, 2012-10, Vol.22 (5), p.660-669</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-eb53269af809b1f1a9577e7f7dfee99b7c572c143168f03b44522ab957a81a8c3</citedby><cites>FETCH-LOGICAL-c419t-eb53269af809b1f1a9577e7f7dfee99b7c572c143168f03b44522ab957a81a8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.sbi.2012.08.007$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23000032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Osawa, Masanori</creatorcontrib><creatorcontrib>Takeuchi, Koh</creatorcontrib><creatorcontrib>Ueda, Takumi</creatorcontrib><creatorcontrib>Nishida, Noritaka</creatorcontrib><creatorcontrib>Shimada, Ichio</creatorcontrib><title>Functional dynamics of proteins revealed by solution NMR</title><title>Current opinion in structural biology</title><addtitle>Curr Opin Struct Biol</addtitle><description>► Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ► Recent progresses in a variety of NMR techniques are reviewed. ► Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ► NMR applications to functionally relevant protein dynamics are also introduced.
Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been ‘invisible’ with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics.</description><subject>Humans</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Solutions</subject><issn>0959-440X</issn><issn>1879-033X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRbK3-AC-So5fEmXztLp6kWBWqgij0tmw2E9iSj5pNCv33bmn16Gnm8LwvMw9j1wgRAuZ368gVNooB4whEBMBP2BQFlyEkyeqUTUFmMkxTWE3YhXNrAMgxFedsEid-hySeMrEYWzPYrtV1UO5a3Vjjgq4KNn03kG1d0NOWdE1lUOwC19Xjng3eXj8u2Vmla0dXxzljX4vHz_lzuHx_epk_LEOTohxCKrIkzqWuBMgCK9Qy45x4xcuKSMqCm4zHBtMEc1FBUqRpFse68JQWqIVJZuz20Osv-h7JDaqxzlBd65a60SlETLl_jGcexQNq-s65niq16W2j-51CUHthaq28MLUXpkAoL8xnbo71Y9FQ-Zf4NeSB-wNA_smtpV45Y6k1VNqezKDKzv5T_wP1EHp1</recordid><startdate>201210</startdate><enddate>201210</enddate><creator>Osawa, Masanori</creator><creator>Takeuchi, Koh</creator><creator>Ueda, Takumi</creator><creator>Nishida, Noritaka</creator><creator>Shimada, Ichio</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>201210</creationdate><title>Functional dynamics of proteins revealed by solution NMR</title><author>Osawa, Masanori ; Takeuchi, Koh ; Ueda, Takumi ; Nishida, Noritaka ; Shimada, Ichio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-eb53269af809b1f1a9577e7f7dfee99b7c572c143168f03b44522ab957a81a8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Humans</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Osawa, Masanori</creatorcontrib><creatorcontrib>Takeuchi, Koh</creatorcontrib><creatorcontrib>Ueda, Takumi</creatorcontrib><creatorcontrib>Nishida, Noritaka</creatorcontrib><creatorcontrib>Shimada, Ichio</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>Osawa, Masanori</au><au>Takeuchi, Koh</au><au>Ueda, Takumi</au><au>Nishida, Noritaka</au><au>Shimada, Ichio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional dynamics of proteins revealed by solution NMR</atitle><jtitle>Current opinion in structural biology</jtitle><addtitle>Curr Opin Struct Biol</addtitle><date>2012-10</date><risdate>2012</risdate><volume>22</volume><issue>5</issue><spage>660</spage><epage>669</epage><pages>660-669</pages><issn>0959-440X</issn><eissn>1879-033X</eissn><abstract>► Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ► Recent progresses in a variety of NMR techniques are reviewed. ► Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ► NMR applications to functionally relevant protein dynamics are also introduced.
Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been ‘invisible’ with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23000032</pmid><doi>10.1016/j.sbi.2012.08.007</doi><tpages>10</tpages></addata></record> |
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subjects | Humans Nuclear Magnetic Resonance, Biomolecular - methods Proteins - chemistry Proteins - metabolism Solutions |
title | Functional dynamics of proteins revealed by solution NMR |
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