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Journal ArticleDOI

Analysis of the amino acid sequence of peptides by mass spectrometry. An ion notation proposal.

TLDR
A new nomenclature is proposed that allows a precise and concise description of mass spectrometric fragments derived from peptides by specifically accommodating extended or unusual amino acid residues, cyclic- and cyclodepsipeptides, and residues contained in branches of the main chain.
Abstract
A new nomenclature is proposed that allows a precise and concise description of mass spectrometric fragments derived from peptides. The nomenclature differs from existing methods by specifically accommodating (1) extended or unusual amino acid residues, (2) cyclic- and cyclodepsipeptides, and (3) residues contained in branches of the main chain.

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Citations
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Journal ArticleDOI

Protein mass spectrometry: applications to analytical biotechnology

TL;DR: An overview of the applications of protein mass spectrometry in the area of analytical biotechnology, particularly as related to biopharmaceutical research and development is presented.
Journal ArticleDOI

A nomenclature system for labeling cyclic peptide fragments

TL;DR: The proposed nomenclature system is applicable to a wide range of cyclic peptides, including depsipeptides, cycling peptides containing modified or unusual amino acids, cycled peptides bearing a linear peptide moiety, and cyclics that are introduced into the gas phase as metal-ion cationized species.
Journal ArticleDOI

The binding protein of corticotropin-releasing factor: ligand-binding site and subunit structure.

TL;DR: It was concluded that the sequence of amino acid residues 23–36 of CRFBP is involved in ligand binding, and the data are in support of an antiparallel alignment of the photoprobe with the amino acids residues 23-36 of theCRFBP monomer.
Journal ArticleDOI

Isolation and structure determination of malevamide E, a dolastatin 14 analogue, from the marine cyanobacterium Symploca laete-viridis.

TL;DR: A new depsipeptide, malevamide E (1), was isolated from field-collected colonies of the filamentous cyanobacterium Symploca laete-viridis, and demonstrated a dose-dependent inhibition of store-operated Ca(2+) entry in thapsigargin-treated human embryonic kidney (HEK) cells, indicating an inhibitory effect on Ca (2+) release-activated Ca( 2+) (CRAC) channels.
References
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Journal ArticleDOI

The structure of cyanoginosin-LA, a cyclic heptapeptide toxin from the cyanobacterium Microcystis aeruginosa

TL;DR: The structure of cyanoginosin-LA (previously referred to by us as toxin BE-4) is cyclo(-D-Ala- L-Leu-erythro-β-methyl-D-isoAsp-L-AlA-Adda- D-Glu-N-methyldehydroAla) and a new nomenclature for the related toxins of Microcystis aeruginosa is discussed.
Journal ArticleDOI

Elucidation by FAB-MS of the structure of a new cardioactive peptide from Aplysia.

TL;DR: The purification and sequence determination by a combination of microprotein chemistry and fast atom bombardment mass spectrometry FAB–MS3,4 of one of the small class of cardioactive peptides, termed SCPB is described.
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