Bicelle samples for solid-state NMR of membrane proteins
Magnetically aligned bicelles are an excellent medium for structure determination of isotopically labeled membrane proteins by solid-state NMR spectroscopy. Bicelles are a mixture of long- and short-chain phospholipids that form bilayers in an aqueous medium and align spontaneously in a high magneti...
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| Veröffentlicht in: | Nature protocols 2007-10, Vol.2 (10), p.2332-2338 |
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| creator | De Angelis, Anna A Opella, Stanley J |
| description | Magnetically aligned bicelles are an excellent medium for structure determination of isotopically labeled membrane proteins by solid-state NMR spectroscopy. Bicelles are a mixture of long- and short-chain phospholipids that form bilayers in an aqueous medium and align spontaneously in a high magnetic field, for example that of an NMR spectrometer with a
1
H resonance frequency between 400 and 900 MHz. Importantly, membrane proteins have been shown to be fully functional in these fully hydrated, planar bilayers under physiological conditions of pH and temperature. We describe a protocol for preparing stable protein-containing bicelles samples that yield high-resolution solid-state NMR spectra. Depending on the details of the protein and its behavior in the lipids, the time for sample preparation can vary from a few hours to several days. |
| doi_str_mv | 10.1038/nprot.2007.329 |
| format | Article |
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1
H resonance frequency between 400 and 900 MHz. Importantly, membrane proteins have been shown to be fully functional in these fully hydrated, planar bilayers under physiological conditions of pH and temperature. We describe a protocol for preparing stable protein-containing bicelles samples that yield high-resolution solid-state NMR spectra. Depending on the details of the protein and its behavior in the lipids, the time for sample preparation can vary from a few hours to several days.</description><identifier>ISSN: 1754-2189</identifier><identifier>EISSN: 1750-2799</identifier><identifier>DOI: 10.1038/nprot.2007.329</identifier><identifier>PMID: 17947974</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Analytical Chemistry ; Biological Techniques ; Biomedical and Life Sciences ; Computational Biology/Bioinformatics ; Life Sciences ; Lipid Bilayers - chemistry ; Lipid membranes ; Lipids ; Magnetic fields ; Membrane proteins ; Membrane Proteins - chemistry ; Membranes ; Membranes, Artificial ; Microarrays ; Nuclear Magnetic Resonance, Biomolecular - methods ; Organic Chemistry ; Physiological aspects ; Physiology ; Protein Folding ; Proteins ; Protocol ; Resonance ; Sample preparation ; Spectroscopy ; Structure</subject><ispartof>Nature protocols, 2007-10, Vol.2 (10), p.2332-2338</ispartof><rights>Springer Nature Limited 2007</rights><rights>COPYRIGHT 2007 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Oct 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c501t-cb02b024d52d12c2059df039cd4a1be55eb0b4c5bf66c13e6a33d2fc0b23b1a3</citedby><cites>FETCH-LOGICAL-c501t-cb02b024d52d12c2059df039cd4a1be55eb0b4c5bf66c13e6a33d2fc0b23b1a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nprot.2007.329$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nprot.2007.329$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17947974$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Angelis, Anna A</creatorcontrib><creatorcontrib>Opella, Stanley J</creatorcontrib><title>Bicelle samples for solid-state NMR of membrane proteins</title><title>Nature protocols</title><addtitle>Nat Protoc</addtitle><addtitle>Nat Protoc</addtitle><description>Magnetically aligned bicelles are an excellent medium for structure determination of isotopically labeled membrane proteins by solid-state NMR spectroscopy. Bicelles are a mixture of long- and short-chain phospholipids that form bilayers in an aqueous medium and align spontaneously in a high magnetic field, for example that of an NMR spectrometer with a
1
H resonance frequency between 400 and 900 MHz. Importantly, membrane proteins have been shown to be fully functional in these fully hydrated, planar bilayers under physiological conditions of pH and temperature. We describe a protocol for preparing stable protein-containing bicelles samples that yield high-resolution solid-state NMR spectra. 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chemistry</topic><topic>Lipid membranes</topic><topic>Lipids</topic><topic>Magnetic fields</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membranes</topic><topic>Membranes, Artificial</topic><topic>Microarrays</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Organic Chemistry</topic><topic>Physiological aspects</topic><topic>Physiology</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Protocol</topic><topic>Resonance</topic><topic>Sample preparation</topic><topic>Spectroscopy</topic><topic>Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Angelis, Anna A</creatorcontrib><creatorcontrib>Opella, Stanley J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Middle School</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature protocols</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Angelis, Anna A</au><au>Opella, Stanley J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bicelle samples for solid-state NMR of membrane proteins</atitle><jtitle>Nature protocols</jtitle><stitle>Nat Protoc</stitle><addtitle>Nat Protoc</addtitle><date>2007-10-01</date><risdate>2007</risdate><volume>2</volume><issue>10</issue><spage>2332</spage><epage>2338</epage><pages>2332-2338</pages><issn>1754-2189</issn><eissn>1750-2799</eissn><abstract>Magnetically aligned bicelles are an excellent medium for structure determination of isotopically labeled membrane proteins by solid-state NMR spectroscopy. Bicelles are a mixture of long- and short-chain phospholipids that form bilayers in an aqueous medium and align spontaneously in a high magnetic field, for example that of an NMR spectrometer with a
1
H resonance frequency between 400 and 900 MHz. Importantly, membrane proteins have been shown to be fully functional in these fully hydrated, planar bilayers under physiological conditions of pH and temperature. We describe a protocol for preparing stable protein-containing bicelles samples that yield high-resolution solid-state NMR spectra. Depending on the details of the protein and its behavior in the lipids, the time for sample preparation can vary from a few hours to several days.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>17947974</pmid><doi>10.1038/nprot.2007.329</doi><tpages>7</tpages></addata></record> |
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| subjects | Analytical Chemistry Biological Techniques Biomedical and Life Sciences Computational Biology/Bioinformatics Life Sciences Lipid Bilayers - chemistry Lipid membranes Lipids Magnetic fields Membrane proteins Membrane Proteins - chemistry Membranes Membranes, Artificial Microarrays Nuclear Magnetic Resonance, Biomolecular - methods Organic Chemistry Physiological aspects Physiology Protein Folding Proteins Protocol Resonance Sample preparation Spectroscopy Structure |
| title | Bicelle samples for solid-state NMR of membrane proteins |
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