Linked Life Data

19377941

Source:http://linkedlifedata.com/resource/pubmed/id/19377941

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-4-20
pubmed:abstractText
Matrix-assisted laser desorption ionization or electrospray ionization mass spectrometry combined with differential chemical modification have proven to be versatile tools for epitope mapping as well as for studying diverse protein-protein and protein-ligand interactions. Characterization of a discontinuous or a conformational epitope on an antigen demands the ability to map the three-dimensional protein surface along with the interface of two interacting proteins. Classical methods of differentially derivatizing amino acid residues have been successfully merged with highly sensitive and highly accurate mass spectrometric techniques to rapidly profile the three-dimensional protein surface and determine the surface accessibility of specific amino acid residues. Here we discuss the use of mass spectrometry to characterize discontinuous or conformational epitopes by studying antigen-antibody interactions. The steps involved in epitope mapping approaches using differential chemical modification and H/D exchange on the antigen are discussed in detail, with particular emphasis on the experimental protocols.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
524
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-34
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Epitope mapping by differential chemical modification of antigens.
pubmed:affiliation
Laboratory of Structural Biology, National Institute of Environmental Health Sciences, NIH, DHHS, 111 T.W. Alexander Drive, PO Box 12233, Research Triangle Park, NC 27709, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Intramural