High-performance solvent suppression for proton detected solid-state NMR
High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by puls...
Gespeichert in:
| Veröffentlicht in: | Journal of magnetic resonance (1997) 2008-05, Vol.192 (1), p.167-172 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 172 |
|---|---|
| container_issue | 1 |
| container_start_page | 167 |
| container_title | Journal of magnetic resonance (1997) |
| container_volume | 192 |
| creator | Zhou, Donghua H. Rienstra, Chad M. |
| description | High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by pulsed field gradients (PFG) and/or saturation pulses. Here we report a high-performance solvent suppression method that attenuates multiple solvent signals simultaneously by more than a factor of 10,000, achieved by an optimized combination of homospoil gradients and supercycled saturation pulses. This method, which we call Multiple Intense Solvent Suppression Intended for Sensitive Spectroscopic Investigation of Protonated Proteins, Instantly (MISSISSIPPI), can be applied without a PFG probe. It opens up new opportunities for two-dimensional heteronuclear correlation spectroscopy of hydrated proteins at
natural abundance as well as high-sensitivity and multi-dimensional experimental investigation of protein–solvent interactions. |
| doi_str_mv | 10.1016/j.jmr.2008.01.012 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2443633</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1090780708000438</els_id><sourcerecordid>69179139</sourcerecordid><originalsourceid>FETCH-LOGICAL-c515t-2d61bb1730d6a207fd30ff1c06c4395dc7cb80910d5c7d735de8ef33a6a55b93</originalsourceid><addsrcrecordid>eNp9kEFr3DAQhUVJaNK0P6CX4lNu3s5YK8kmEAhL2y0kKZTchSyNEy225Urehf77aLtL014CAzMwb94bPsY-IiwQUH7eLDZDXFQA9QIwV_WGnSM0soRayJM_M5SqBnXG3qW0AUAUCt6yM6wrJVGJc7Ze-8encqLYhTiY0VKRQr-jcS7SdpoipeTDWORlMcUw59HRTHYmt9d5V6bZzFTc3_18z0470yf6cOwX7OHrl4fVurz98e376ua2tALFXFZOYtui4uCkqUB1jkPXoQVpl7wRzirb1tAgOGGVU1w4qqnj3EgjRNvwC3Z9sJ227UDO5k-j6fUU_WDibx2M1_9vRv-kH8NOV8sll5xng8ujQQy_tpRmPfhkqe_NSGGbtGxQNcj3SXgQ2hhSitT9DUHQe_x6ozN-vcevAXNV-ebTv9-9XBx5Z8HVQUAZ0c5T1Ml6ytidjxmrdsG_Yv8MI9GXyQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69179139</pqid></control><display><type>article</type><title>High-performance solvent suppression for proton detected solid-state NMR</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Zhou, Donghua H. ; Rienstra, Chad M.</creator><creatorcontrib>Zhou, Donghua H. ; Rienstra, Chad M.</creatorcontrib><description>High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by pulsed field gradients (PFG) and/or saturation pulses. Here we report a high-performance solvent suppression method that attenuates multiple solvent signals simultaneously by more than a factor of 10,000, achieved by an optimized combination of homospoil gradients and supercycled saturation pulses. This method, which we call Multiple Intense Solvent Suppression Intended for Sensitive Spectroscopic Investigation of Protonated Proteins, Instantly (MISSISSIPPI), can be applied without a PFG probe. It opens up new opportunities for two-dimensional heteronuclear correlation spectroscopy of hydrated proteins at
natural abundance as well as high-sensitivity and multi-dimensional experimental investigation of protein–solvent interactions.</description><identifier>ISSN: 1090-7807</identifier><identifier>EISSN: 1096-0856</identifier><identifier>DOI: 10.1016/j.jmr.2008.01.012</identifier><identifier>PMID: 18276175</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Carbon Isotopes ; Magic-angle spinning NMR ; Natural abundance ; Nerve Tissue Proteins - chemistry ; Nitrogen Isotopes ; Nuclear Magnetic Resonance, Biomolecular - methods ; Protein–solvent interactions ; Proton detection ; Protons ; Solvent suppression ; Solvents - chemistry</subject><ispartof>Journal of magnetic resonance (1997), 2008-05, Vol.192 (1), p.167-172</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c515t-2d61bb1730d6a207fd30ff1c06c4395dc7cb80910d5c7d735de8ef33a6a55b93</citedby><cites>FETCH-LOGICAL-c515t-2d61bb1730d6a207fd30ff1c06c4395dc7cb80910d5c7d735de8ef33a6a55b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1090780708000438$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18276175$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Donghua H.</creatorcontrib><creatorcontrib>Rienstra, Chad M.</creatorcontrib><title>High-performance solvent suppression for proton detected solid-state NMR</title><title>Journal of magnetic resonance (1997)</title><addtitle>J Magn Reson</addtitle><description>High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by pulsed field gradients (PFG) and/or saturation pulses. Here we report a high-performance solvent suppression method that attenuates multiple solvent signals simultaneously by more than a factor of 10,000, achieved by an optimized combination of homospoil gradients and supercycled saturation pulses. This method, which we call Multiple Intense Solvent Suppression Intended for Sensitive Spectroscopic Investigation of Protonated Proteins, Instantly (MISSISSIPPI), can be applied without a PFG probe. It opens up new opportunities for two-dimensional heteronuclear correlation spectroscopy of hydrated proteins at
natural abundance as well as high-sensitivity and multi-dimensional experimental investigation of protein–solvent interactions.</description><subject>Carbon Isotopes</subject><subject>Magic-angle spinning NMR</subject><subject>Natural abundance</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nitrogen Isotopes</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Protein–solvent interactions</subject><subject>Proton detection</subject><subject>Protons</subject><subject>Solvent suppression</subject><subject>Solvents - chemistry</subject><issn>1090-7807</issn><issn>1096-0856</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFr3DAQhUVJaNK0P6CX4lNu3s5YK8kmEAhL2y0kKZTchSyNEy225Urehf77aLtL014CAzMwb94bPsY-IiwQUH7eLDZDXFQA9QIwV_WGnSM0soRayJM_M5SqBnXG3qW0AUAUCt6yM6wrJVGJc7Ze-8encqLYhTiY0VKRQr-jcS7SdpoipeTDWORlMcUw59HRTHYmt9d5V6bZzFTc3_18z0470yf6cOwX7OHrl4fVurz98e376ua2tALFXFZOYtui4uCkqUB1jkPXoQVpl7wRzirb1tAgOGGVU1w4qqnj3EgjRNvwC3Z9sJ227UDO5k-j6fUU_WDibx2M1_9vRv-kH8NOV8sll5xng8ujQQy_tpRmPfhkqe_NSGGbtGxQNcj3SXgQ2hhSitT9DUHQe_x6ozN-vcevAXNV-ebTv9-9XBx5Z8HVQUAZ0c5T1Ml6ytidjxmrdsG_Yv8MI9GXyQ</recordid><startdate>20080501</startdate><enddate>20080501</enddate><creator>Zhou, Donghua H.</creator><creator>Rienstra, Chad M.</creator><general>Elsevier Inc</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>5PM</scope></search><sort><creationdate>20080501</creationdate><title>High-performance solvent suppression for proton detected solid-state NMR</title><author>Zhou, Donghua H. ; Rienstra, Chad M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c515t-2d61bb1730d6a207fd30ff1c06c4395dc7cb80910d5c7d735de8ef33a6a55b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Carbon Isotopes</topic><topic>Magic-angle spinning NMR</topic><topic>Natural abundance</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nitrogen Isotopes</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Protein–solvent interactions</topic><topic>Proton detection</topic><topic>Protons</topic><topic>Solvent suppression</topic><topic>Solvents - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhou, Donghua H.</creatorcontrib><creatorcontrib>Rienstra, Chad M.</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>PubMed Central (Full Participant titles)</collection><jtitle>Journal of magnetic resonance (1997)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Donghua H.</au><au>Rienstra, Chad M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High-performance solvent suppression for proton detected solid-state NMR</atitle><jtitle>Journal of magnetic resonance (1997)</jtitle><addtitle>J Magn Reson</addtitle><date>2008-05-01</date><risdate>2008</risdate><volume>192</volume><issue>1</issue><spage>167</spage><epage>172</epage><pages>167-172</pages><issn>1090-7807</issn><eissn>1096-0856</eissn><abstract>High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by pulsed field gradients (PFG) and/or saturation pulses. Here we report a high-performance solvent suppression method that attenuates multiple solvent signals simultaneously by more than a factor of 10,000, achieved by an optimized combination of homospoil gradients and supercycled saturation pulses. This method, which we call Multiple Intense Solvent Suppression Intended for Sensitive Spectroscopic Investigation of Protonated Proteins, Instantly (MISSISSIPPI), can be applied without a PFG probe. It opens up new opportunities for two-dimensional heteronuclear correlation spectroscopy of hydrated proteins at
natural abundance as well as high-sensitivity and multi-dimensional experimental investigation of protein–solvent interactions.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18276175</pmid><doi>10.1016/j.jmr.2008.01.012</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1090-7807 |
| ispartof | Journal of magnetic resonance (1997), 2008-05, Vol.192 (1), p.167-172 |
| issn | 1090-7807 1096-0856 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2443633 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Carbon Isotopes Magic-angle spinning NMR Natural abundance Nerve Tissue Proteins - chemistry Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Protein–solvent interactions Proton detection Protons Solvent suppression Solvents - chemistry |
| title | High-performance solvent suppression for proton detected solid-state NMR |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-15T13%3A35%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=High-performance%20solvent%20suppression%20for%20proton%20detected%20solid-state%20NMR&rft.jtitle=Journal%20of%20magnetic%20resonance%20(1997)&rft.au=Zhou,%20Donghua%20H.&rft.date=2008-05-01&rft.volume=192&rft.issue=1&rft.spage=167&rft.epage=172&rft.pages=167-172&rft.issn=1090-7807&rft.eissn=1096-0856&rft_id=info:doi/10.1016/j.jmr.2008.01.012&rft_dat=%3Cproquest_pubme%3E69179139%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69179139&rft_id=info:pmid/18276175&rft_els_id=S1090780708000438&rfr_iscdi=true |