Electrostatic interactions contribute to the control of intramolecular thiol–disulfide isomerization in a protein

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Abstract:

of structural factors and of electrostatic interactions with the environment on the outcome of thiol–disulfide exchange reactions were investigated in a mutated immunoglobulin domain (I27*) under mechanical stress.

SEEK ID: https://publications.h-its.org/publications/1320

SEEK ID: https://publications.h-its.org/publications/1320

PubMed ID: 34792054

DOI: 10.1039/d1cp03129e

Research Groups: Molecular Biomechanics

Publication type: Journal

Journal: Physical Chemistry Chemical Physics

Publisher: Royal Society of Chemistry (RSC)

Citation: Phys Chem Chem Phys,23(46):26366-26375.

Date Published: 2021

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Registered Mode: manually

Authors: Denis Maag, Marina Putzu, Claudia L. Gómez-Flores, Frauke Gräter, Marcus Elstner, Tomáš Kubař

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Citation
Maag, D., Putzu, M., Gómez-Flores, C. L., Gräter, F., Elstner, M., & Kubař, T. (2021). Electrostatic interactions contribute to the control of intramolecular thiol–disulfide isomerization in a protein. In Physical Chemistry Chemical Physics (Vol. 23, Issue 46, pp. 26366–26375). Royal Society of Chemistry (RSC). https://doi.org/10.1039/d1cp03129e
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Created: 22nd Nov 2021 at 05:33

Last updated: 5th Mar 2024 at 21:24

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