Linked Life Data

10472044

Source:http://linkedlifedata.com/resource/pubmed/id/10472044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-10-20
pubmed:abstractText
The high resolution structure of the gramicidin A channel has been determined in a lamellar phase environment using solid-state NMR spectroscopy. While the fold is similar to previous characterizations, channel function is exquisitely dependent on structural detail. There is essentially no structural change upon cation binding and no significant change in dynamics. The cations appear to be adequately solvated in their binding site by no more than two carbonyls and no fewer than three water molecules at any one time. The relatively large number of water molecules allows for geometric flexibility and little selectivity among monovalent cations. However, the dehydration energies of cations clearly explain the selectivity for monovalent versus divalent cations. Moreover, the binding site is shown to be delocalized, resulting in a shallow potential energy well so that efficient cation conductance can be realized. The potential energy barrier at the bilayer centre has been shown to be rate limiting under certain circumstances through a correlation between conductance and the electrostatic interactions between cations at the gramicidin monomer-monomer junction and the indole dipole moments at the lipid-water interface. The dynamics are functionally important. The time-scale for carbonyl fluctuations about the C alpha-C alpha axis and kinetic rates for cation movement in the channel are the same, suggesting a correlation between molecular dynamics and kinetics. These functional correlations will be described in light of the recent K+ channel structure and the biological challenge to achieve both selectivity and efficiency.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1528-2511
pubmed:author
pubmed:issnType
Print
pubmed:volume
225
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4-16; discussion 16-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Correlations of structure, dynamics and function in the gramicidin channel by solid-state NMR spectroscopy.
pubmed:affiliation
Department of Chemistry, Florida State University, Tallahassee 32310, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't