Comparison of the pH‐dependent formation of His and Cys heptapeptide complexes of nickel(II), copper(II), and zinc(II) as determined by ion mobility‐mass spectrometry-Reference-Cited by-同舟云学术

Comparison of the pH‐dependent formation of His and Cys heptapeptide complexes of nickel(II), copper(II), and zinc(II) as determined by ion mobility‐mass spectrometry

Published:2020-02-06 Issue:3 Volume:55 Page:
ISSN:1076-5174
Container-title:Journal of Mass Spectrometry
language:en
Short-container-title:J Mass Spectrom

Author:

Yousef Enas N.¹,Angel Laurence A.¹^ORCID

Affiliation:

1. Department of Chemistry Texas A&M University‐Commerce Commerce Texas 75428 USA

Funder

National Science Foundation

Connecticut Department of Energy and Environmental Protection

Welch Foundation

Publisher

Wiley

Subject

Spectroscopy

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jms.4489

Reference62 articles.

1. The multiple conformational charge states of zinc(II) coordination by 2His‐2Cys oligopeptide investigated by ion mobility‐mass spectrometry, density functional theory and theoretical collision cross sections

2. Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides

3. Analysis of Methanobactin from Methylosinus Trichosporium OB3b via Ion Mobility Mass Spectrometry

4. Binding Selectivity of Methanobactin from Methylosinus trichosporium OB3b for Copper(I), Silver(I), Zinc(II), Nickel(II), Cobalt(II), Manganese(II), Lead(II), and Iron(II)

5. The pH Dependent Cu(II) and Zn(II) Binding Behavior of an Analog Methanobactin Peptide

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