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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2006-8-21
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pubmed:abstractText |
This review focuses upon the application of solution NMR methods to multispan integral membrane proteins, particularly with respect to determination of global folds by this approach. Practical methods are described along with the special difficulties that confront the application of solution NMR to proteins that dwell in the netherworld of the lipid bilayer.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0749-1581
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2006 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:volume |
44 Spec No
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S24-40
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:16826539-Amino Acid Sequence,
pubmed-meshheading:16826539-Detergents,
pubmed-meshheading:16826539-Lipid Bilayers,
pubmed-meshheading:16826539-Membrane Proteins,
pubmed-meshheading:16826539-Micelles,
pubmed-meshheading:16826539-Molecular Sequence Data,
pubmed-meshheading:16826539-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16826539-Protein Folding,
pubmed-meshheading:16826539-Solutions,
pubmed-meshheading:16826539-Solvents
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pubmed:year |
2006
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pubmed:articleTitle |
Solution NMR of membrane proteins: practice and challenges.
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pubmed:affiliation |
Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232-8725, USA. chuck.sanders@vanderbilt.edu
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Extramural
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