Linked Life Data

17046396

Source:http://linkedlifedata.com/resource/pubmed/id/17046396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-10-18
pubmed:abstractText
Hydrogen/deuterium (H/D) exchange analyzed by mass spectrometry (HXMS) is a valuable tool for the investigation of protein conformation and dynamics. After exchange, the sample is generally submitted to electrospray ionization for mass analysis. Matrix-assisted laser desorption ionization (MALDI) has been used in a limited number of studies but has several significant advantages that include simplification of the spectra attributable to a predominance of singly charged ions, speed of analysis, sensitivity, and low H/D back-exchange level. MALDI-HXMS has been used to study amyloid aggregates from the HET-s prion protein. Our results underline the ability of this method to determine solvent accessibility within the amyloid aggregates, reaching a resolution of one to four amino acids. To achieve a complete peptide mass fingerprint of the protein, we have taken benefits of an ion trap operating in liquid chromatography-MS/MS mode. MALDI time-of-flight-MS was then used to determine deuterium incorporation within each peptide along the sequence of HET-s. The combined advantages of these two instruments yield a suitable solution for HXMS experiments that require highly resolved peptide mass fingerprints, high sensitivity, and speed of analysis for deuterium incorporation measurements.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
413
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Hydrogen-deuterium exchange analyzed by matrix-assisted laser desorption-ionization mass spectrometry and the HET-s prion model.
pubmed:affiliation
Swiss Federal Institute of Technology, ETH, Department of Chemistry and Applied Biosciences, Zurich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't