Non-covalent interactions between unsolvated peptides: Helical complexes based on acid-base interactions
Article Abstract:
The conformation of the protonated complex formed between AcA7KA6KK and AcEA7EA7, helical alanine-based peptides that incorporate glutamic acid (E) and lysine (K) is examined using ion-mobility mass spectroscopy. Designed interactions between the acidic E and basic K residues help to stabilize the complex, which is generated by electrospray and studied in the gas phase.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
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Noncovalent interactions between unsolvated peptides: Dissociation of helical and globular peptide complexes
Article Abstract:
Electrospray mass spectrometry and ion mobility measurements are used to study the thermally activated unimolecular dissociation of the unsolvated complexes of helical and globular alanine/glycine-based peptides. Activation energies and entropies are determined from the rates constants measured as a function of temperature.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2003
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Fragmentation mechanisms of product ions from protonated tripeptides
Article Abstract:
Dissociation chemistries of the primary fragment ions from the tripeptides, GAG and AGG, were examined both experimentally and theoretically, and compared with those from GGG. Findings derived from the study with GAG and AGG are presented.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
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