Computational Study of Matrix−Peptide Interactions in MALDI Mass Spectrometry: Interactions of 2,5- and 3,5-Dihydroxybenzoic Acid with the Tripeptide Valine−Proline−Leucine
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas 76019-0065
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp058257c
Reference21 articles.
1. Ion formation in MALDI mass spectrometry
2. Secondary ion-molecule reactions in matrix-assisted laser desorption/ionization
3. Ionization processes in matrix-assisted laser desorption/ionization mass spectrometry: Matrix-dependent formation of [M + H]+ vs [M + Na]+ ions of small peptides and some mechanistic comments
4. Ionization energy reductions in small 2,5-dihydroxybenzoic acid-proline clusters
5. Arginine/2,5-Dihydroxybenzoic Acid Clusters: An Experimental and Computational Study of the Gas-Phase and Solid-State Systems
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2. MALDI Ionization Mechanisms: An Overview;Electrospray and MALDI Mass Spectrometry;2012-11-27
3. Molecular dynamics simulations of matrix assisted laser desorption ionization: Matrix–analyte interactions;Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms;2011-07
4. A density functional theory (DFT) study on gas-phase proton transfer reactions of derivatized and underivatized peptide ions generated by matrix-assisted laser desorption ionization;Journal of the American Society for Mass Spectrometry;2009-07-01
5. A comparative computational study of matrix-peptide interactions in MALDI mass spectrometry: the interaction of four tripeptides with the MALDI matrices 2,5-dihyroxybenzoic acid, α-cyano-4-hydroxy-cinnamic acid and 3,5-dihyroxybenzoic acid;Molecular Physics;2009-04-20
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