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Frontispiece: What Are We Missing by Not Measuring the Net Charge of Proteins?
Author(s) -
Zahler Collin T.,
Shaw Bryan F.
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201983261
Subject(s) - isoelectric point , charge (physics) , electrostatics , net (polyhedron) , chemical physics , chemistry , crystallography , nanotechnology , physics , materials science , mathematics , biochemistry , quantum mechanics , geometry , enzyme
The net electrostatic charge of most folded proteins has never been measured in solution at pH values different from the isoelectric point. The authors discuss how measuring the net electrostatic charge Z of folded, solvated proteins can provide new information about fundamental electrostatic properties of metalloproteins or about processes in which they are involved, for example, electron transfer or metal coordination. For more details see the Concept by B. F. Shaw and C. T. Zahler on page 7581 ff.