Linked Life Data

20533847

Source:http://linkedlifedata.com/resource/pubmed/id/20533847

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2010-6-24
pubmed:abstractText
The conformation of model [Arg(Ala)(4)X(Ala)(4)Lys+2H](2+) and [Arg(Gly)(4)X(Gly)(4)Lys+2H](2+) peptides has been systematically investigated as a function of the central amino acid X through a combined experimental and theoretical approach. Mass spectrometry-based ion mobility measurements have been performed together with conformational sampling using replica-exchange molecular dynamics to probe the influence of each amino acid on the stable peptide conformation. Satisfactory agreement is obtained between measured and calculated diffusion cross section distributions. The results confirm the propensity of alanine-based peptides to form alpha-helices in the gas phase, differences between peptides arising from the local arrangement of the central side chain with respect to the charged ends. More generally, we find that charge solvation plays a major role in secondary structure stabilization, especially in the case of glycine-based peptides. The rich variety of conformations exhibited by the latter is qualitatively captured by the simulations. This work illustrates the potentiality of such combined experimental/theoretical strategy to determine peptide secondary structures. The present polyalanine and polyglycine peptides also offer a series of benchmark systems for future conformation-resolved studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1520-5215
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6888-96
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Conformation of polyalanine and polyglycine dications in the gas phase: insight from ion mobility spectrometry and replica-exchange molecular dynamics.
pubmed:affiliation
Université de Lyon, F-69622, Lyon, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't