Linked Life Data

19595987

Source:http://linkedlifedata.com/resource/pubmed/id/19595987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2009-8-24
pubmed:abstractText
The membrane location of two fragments in two different K(+)-channels, the KvAP (from Aeropyrum pernix) and the HsapBK (human) corresponding to the putative "paddle" domains, has been investigated by CD, fluorescence and NMR spectroscopy. Both domains interact with q = 0.5 phospholipid bicelles, DHPC micelles and with POPC vesicles. CD spectra demonstrate that both peptides become largely helical in the presence of phospholipid bicelles. Fluorescence quenching studies using soluble acrylamide or lipid-attached doxyl-groups show that the arginine-rich domains are located within the bilayered region in phospholipid bicelles. Nuclear magnetic relaxation parameters, T(1) and (13)C-(1)H NOE, for DMPC in DMPC/DHPC bicelles and for DHPC in micelles showed that the lipid acyl chains in the bicelles become less flexible in the presence of either of the fragments. An even more pronounced effect is seen on the glycerol carbons. (2)H NMR spectra of magnetically aligned bicelles showed that the peptide derived from KvAP had no or little effect on bilayer order, while the peptide derived from HsapBK had the effect of lowering the order of the bilayer. The present study demonstrates that the fragments derived from the full-length proteins interact with the bilayered interior of model membranes, and that they affect both the local mobility and lipid order of model membrane systems.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1788
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1976-86
pubmed:meshHeading
pubmed-meshheading:19595987-Acrylamide, pubmed-meshheading:19595987-Biophysical Phenomena, pubmed-meshheading:19595987-Circular Dichroism, pubmed-meshheading:19595987-Desulfurococcaceae, pubmed-meshheading:19595987-Dimyristoylphosphatidylcholine, pubmed-meshheading:19595987-Humans, pubmed-meshheading:19595987-Ion Channel Gating, pubmed-meshheading:19595987-Large-Conductance Calcium-Activated Potassium Channels, pubmed-meshheading:19595987-Lipid Bilayers, pubmed-meshheading:19595987-Micelles, pubmed-meshheading:19595987-Models, Molecular, pubmed-meshheading:19595987-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:19595987-Phospholipid Ethers, pubmed-meshheading:19595987-Potassium Channels, pubmed-meshheading:19595987-Protein Structure, Tertiary, pubmed-meshheading:19595987-Spectrometry, Fluorescence, pubmed-meshheading:19595987-Tryptophan
pubmed:year
2009
pubmed:articleTitle
Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K(+) channels.
pubmed:affiliation
Center for Biomembrane Research, Department of Biochemistry and Biophysics, The Arrhenius Laboratory, Stockholm University, Stockholm 10691, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't