|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2009-1-8
|
|
pubmed:abstractText |
We show that water-edited solid-state NMR spectroscopy allows for probing global protein conformation and residue-specific solvent accessibility in a lipid bilayer environment. The transfer dynamics can be well described by a general time constant, irrespective of protein topology and lipid environment. This approach was used to follow structural changes in response to protein function in the chimeric potassium channel KcsA-Kv1.3. Data obtained as a function of pH link earlier biochemical data to changes in protein structure in a functional bilayer setting.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
1520-5126
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
14
|
|
pubmed:volume |
131
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
170-6
|
|
pubmed:meshHeading |
pubmed-meshheading:19063626-Bacterial Proteins,
pubmed-meshheading:19063626-Calcium-Binding Proteins,
pubmed-meshheading:19063626-Halorhodopsins,
pubmed-meshheading:19063626-Lipid Bilayers,
pubmed-meshheading:19063626-Models, Chemical,
pubmed-meshheading:19063626-Models, Molecular,
pubmed-meshheading:19063626-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:19063626-Potassium Channels,
pubmed-meshheading:19063626-Sensory Rhodopsins,
pubmed-meshheading:19063626-Water
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy.
|
|
pubmed:affiliation |
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
