HYDROGEN-TRITIUM EXCHANGE TITRATION OF THE HISTIDINE RESIDUES IN BOVINE HEART CYTOCHROME C AND ANALYSIS OF THEIR MICROENVIRONMENT
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1979.tb01958.x/fullpdf
Reference23 articles.
1. Nuclear Magnetic Resonance Titration Curves of Histidine Ring Protons
2. Spectroscopic Studies on the Conformation of Cytochrome c and Apocytochrome c
3. Ferricytochrome c
4. On the Role of Heme in the Formation of the Structure of Cytochrome c
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1. Imidazole C-2 Hydrogen/Deuterium Exchange Reaction at Histidine for Probing Protein Structure and Function with Matrix-Assisted Laser Desorption Ionization Mass Spectrometry;Biochemistry;2014-03-14
2. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry;Journal of Mass Spectrometry;2003-01
3. Hydrogen exchange and the dynamic structure of proteins;Molecular and Cellular Biochemistry;1982
4. Assignment of the metal-histidine ligands from the tritium exchange rate of the histidine C-2 protons in the Cu (II), Zn(II)-superoxide dismutase from Saccharomyces cerevisiae;Carlsberg Research Communications;1980-07
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