Salt Bridge Chemistry Applied to Gas-Phase Peptide Sequencing:  Selective Fragmentation of Sodiated Gas-Phase Peptide Ions Adjacent to Aspartic Acid Residues

1998 ◽  
Vol 120 (13) ◽  
pp. 3188-3195 ◽  
Author(s):  
Sang-Won Lee ◽  
Hyun Sik Kim ◽  
J. L. Beauchamp
Keyword(s):  
Gas Phase ◽  
Aspartic Acid ◽  
Salt Bridge ◽  
Peptide Sequencing ◽  
Peptide Ions

Graph theory-based reaction pathway searches and DFT calculations for the mechanism studies of free radical-initiated peptide sequencing mass spectrometry (FRIPS MS): a model gas-phase reaction of GGR tri-peptide

2020 ◽  
Vol 22 (9) ◽  
pp. 5057-5069 ◽  
Author(s):  
Jae-ung Lee ◽  
Yeonjoon Kim ◽  
Woo Youn Kim ◽  
Han Bin Oh
Keyword(s):  
Graph Theory ◽  
Dft Calculations ◽  
Gas Phase ◽  
Density Functional ◽  
Reaction Pathway ◽  
Peptide Sequencing ◽  
Phase Reaction ◽  
Functional Theory ◽  
Fragmentation Mechanisms ◽  
Gas Phase Fragmentation

A new approach for elucidating gas-phase fragmentation mechanisms is proposed: graph theory-based reaction pathway searches (ACE-Reaction program) and density functional theory (DFT) calculations.

scholarly journals Cooperative Salt Bridge Stabilization of Gas-Phase Zwitterions in Neutral Arginine Clusters

2002 ◽  
Vol 106 (1) ◽  
pp. 32-34 ◽  
Author(s):  
Ryan R. Julian ◽  
J. L. Beauchamp ◽  
William A. Goddard
Keyword(s):  
Gas Phase ◽  
Salt Bridge

Vibrational Signature of Charge Solvation vs Salt Bridge Isomers of Sodiated Amino Acids in the Gas Phase

2004 ◽  
Vol 126 (6) ◽  
pp. 1836-1842 ◽  
Author(s):  
Catherine Kapota ◽  
Joël Lemaire ◽  
Philippe Maître ◽  
Gilles Ohanessian
Keyword(s):  
Amino Acids ◽  
Gas Phase ◽  
Salt Bridge ◽  
Charge Solvation

Generation and Characterization of Gas-Phase Doubly Charged Biradical Peptide Ions (M2+••)

2017 ◽  
Vol 89 (14) ◽  
pp. 7773-7780 ◽  
Author(s):  
Y. L. Elaine Wong ◽  
Xiangfeng Chen ◽  
Ri Wu ◽  
Y. L. Winnie Hung ◽  
Hoi Sze Yeung ◽  
...  
Keyword(s):  
Gas Phase ◽  
Peptide Ions ◽  
Doubly Charged

Specificity profiling of human trypsin-isoenzymes

2018 ◽  
Vol 399 (9) ◽  
pp. 997-1007 ◽  
Author(s):  
Oliver Schilling ◽  
Martin L. Biniossek ◽  
Bettina Mayer ◽  
Brigitta Elsässer ◽  
Hans Brandstetter ◽  
...  
Keyword(s):  
Cancer Therapy ◽  
Aspartic Acid ◽  
Therapeutic Target ◽  
Cleavage Site ◽  
Quantitative Proteomics ◽  
Salt Bridge ◽  
Peptide Libraries ◽  
Peptide Substrates ◽  
Bridge Formation ◽  
Specific Inhibitors

AbstractIn humans, three different trypsin-isoenzymes have been described. Of these, trypsin-3 appears to be functionally different from the others. In order to systematically study the specificity of the trypsin-isoenzymes, we utilized proteome-derived peptide libraries and quantitative proteomics. We found similar specificity profiles dominated by the well-characterized preference for cleavage after lysine and arginine. Especially, trypsin-1 slightly favored lysine over arginine in this position, while trypsin-3 did not discriminate between them. In the P1′ position, which is the residue C-terminal to the cleavage site, we noticed a subtle enrichment of alanine and glycine for all three trypsins and for trypsin-3 there were additional minor P1′ and P2′ preferences for threonine and aspartic acid, respectively. These findings were confirmed by FRET peptide substrates showing different susceptibility to cleavage by different trypsins. The preference of trypsin-3 for aspartic acid in P2′ is explained by salt bridge formation with the unique Arg193. This salt bridge enables and stabilizes a canonical oxyanion conformation by the amides of Ser195 and Arg193, thus manifesting a selective substrate-assisted catalysis. As trypsin-3 has been proposed to be a therapeutic target and marker for cancers, our results may aid the development of specific inhibitors for cancer therapy and diagnostic probes.

Ferrocene Conjugates Containing Diarginine and Aspartic Acid: Salt Bridge Interactions in Water

2009 ◽  
Vol 2009 (29-30) ◽  
pp. 4425-4432 ◽  
Author(s):  
Anas Lataifeh ◽  
Chantelle R. Bondy ◽  
Heinz-Bernhard Kraatz
Keyword(s):  
Aspartic Acid ◽  
Salt Bridge ◽  
Acid Salt

Formation of gas-phase peptide ions and their dissociation in MALDI: Insights from kinetic and ion yield studies

2014 ◽  
Vol 34 (2) ◽  
pp. 94-115 ◽  
Author(s):  
Jeong Hee Moon ◽  
Sohee Yoon ◽  
Yong Jin Bae ◽  
Myung Soo Kim
Keyword(s):  
Gas Phase ◽  
Peptide Ions
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