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ESI‐MS Studies on Prolyl Hydroxylase Domain 2 Reveal a New Metal Binding Site
Author(s) -
Mecinović Jasmin,
Chowdhury Rasheduzzaman,
Liénard Benoît M. R.,
Flashman Emily,
Buck Matthew R. G.,
Oldham Neil J.,
Schofield Christopher J.
Publication year - 2008
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200700233
Subject(s) - mutagenesis , metal , chemistry , binding site , computational biology , domain (mathematical analysis) , enzyme , combinatorial chemistry , stereochemistry , biochemistry , biology , organic chemistry , mutation , gene , mathematics , mathematical analysis
Mild ionisation : Combined ESI‐MS and mutagenesis analyses were used in metal binding studies on a human oxygen‐sensing enzyme. The approach revealed a new metal binding site.