EThcD Benefits for the Sequencing Inside Intramolecular Disulfide Cycles of Amphibian Intact Peptides
Author:
Affiliation:
1. Lomonosov Moscow State University, Department of Organic Chemistry, 119991 Moscow, Russia
2. Department of Medicinal Biochemistry and Biophysics, Division of Molecular Biometry, Karolinska Institutet, 17177 Stockholm, Sweden
Funder
Russian Science Foundation
Publisher
American Chemical Society (ACS)
Subject
Spectroscopy,Structural Biology
Link
https://pubs.acs.org/doi/pdf/10.1021/jasms.3c00127
Reference72 articles.
1. Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy
2. Electrospray Ionization Tandem Mass Spectrometry Sequencing of Novel Skin Peptides from Ranid Frogs Containing Disulfide Bridges
3. Identification and Characterization of Disulfide Bonds in Proteins and Peptides from Tandem MS Data by Use of the MassMatrix MS/MS Search Engine
4. FT‐MS in the de novo top‐down sequencing of natural nontryptic peptides
5. Host-defence peptides from the glandular secretions of amphibians: structure and activity
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1. Assessing the Efficacy of Protease Inactivation for the Preservation of Bioactive Amphibian Skin Peptides;International Journal of Molecular Sciences;2024-08-12
2. EThcD as a Unique Tool for the Top-Down De Novo Sequencing of Intact Natural Ranid Amphibian Peptides;Analytical Chemistry;2024-07-09
3. Tandem Mass Spectrometry de novo Sequencing of the Skin Defense Peptides of the Central Slovenian Agile Frog Rana dalmatina;Molecules;2023-10-16
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