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Site correlations, capacitance, and polarizability from protein protonisation fluctuations

06 September 2021, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

We generalize the Kirkwood-Shumaker theory of protonisation fluctuation for an anisotropic distribution of dissociable charges on a globular protein. The fluctuations of the total charge and the total dipole moment, in contrast to their average values, depend on the same proton occupancy correlator, thus exhibiting a similar dependence also on the solution pH. This has important consequences for the Kirkwood-Shumaker interaction and its dependence on the bathing solution conditions.

Keywords

Charge regulation
Kirkwood-Shumaker interaction
Electrostatics of proteins
Protonisation fluctuations

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Version History

Sep 06, 2021 Version 1

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The content is available under CC BY 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2021-h1kw2
D O I: 10.26434/chemrxiv-2021-h1kw2 [opens in a new tab]

Funding

ARRS
P1-0055
NSFC
12034019

Author’s competing interest statement

The author(s) have declared they have no conflict of interest with regard to this content

Ethics

The author(s) have declared ethics committee/IRB approval is not relevant to this content

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