Sodiation of melittin, cytochrome c, and ubiquitin studied by electrospray mass spectrometry: Stabilities of α-helix and β-sheet in basic solutions-Reference-Cited by-同舟云学术

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Sodiation of melittin, cytochrome c, and ubiquitin studied by electrospray mass spectrometry: Stabilities of α-helix and β-sheet in basic solutions

Published:2024-04 Issue: Volume:498 Page:117212
ISSN:1387-3806
Container-title:International Journal of Mass Spectrometry
language:en
Short-container-title:International Journal of Mass Spectrometry

Author:

Hiraoka Kenzo^ORCID,Ninomiya Satoshi,Rankin-Turner Stephanie,Akashi Satoko

Publisher

Elsevier BV

Reference35 articles.

1. Effects of metal ion adduction on the gas-phase conformations of protein ions;Flick;J. Am. Soc. Mass Spectrom.,2013

2. Site-specific sodiation of peptides studied by pulsed nanoelectrospray ionization;Hiraoka;Int. J. Mass Spectrom.,2023

3. Strong interactions of anionic peptides and alkaline earth metal ions: metal-ion-bound peptides in the gas phase;Hu;J. Am. Chem. Soc.,1992

4. Sodium binding interactions with aliphatic amino acids: a guided ion beam and computational study;Pham;J. Phys. Chem. A,2021

5. Generation and manipulation of sodium cationized peptides in the gas phase;Newton;J. Am. Soc. Mass Spectrom.,2004

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural Phylogenetics with Protein Mass Spectrometry: A Proof-of-Concept;The Protein Journal;2024-07-29

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