Linked Life Data

20455530

Source:http://linkedlifedata.com/resource/pubmed/id/20455530

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2010-5-20
pubmed:abstractText
Ab initio MD simulations on a polyglycine helix and water-wire expressed under periodic boundary conditions have created a channel that supports proton transfer up to distances of 10.5 A. The effect of varying the density of water molecules in the channel has been investigated. A range of cationic states are identified with widely varying lifetimes. The mechanism of proton transport in this model shares some features with the simulations reported for bulk water, with, e.g., the hydrogen bond distance shortening in the time period leading up to successful proton transfer. However, there are also some important differences such as the observation of a heightened number of proton rattling events. We also observe that the helix plays an important role in directing the behavior of the water wire: the most active proton transport regions of the water-wire are found in areas where the helix is most tightly coiled. Finally, we report on the effects of different DFT functionals to model a water-wire and on the importance of including dispersion corrections to stabilize the alpha-helical structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1520-5207
pubmed:author
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7047-55
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Simulating proton transport through a simplified model for trans-membrane proteins.
pubmed:affiliation
School of Chemistry and EaSTCHEM Research School, The University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, EH9 3JJ, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't