DOI > 10.5291/ILL-DATA.8-05-440

This proposal is publicly available since 09/17/2024

Title

The influence of crowding, cosolvents and high pressure on protein dynamics

Abstract

The enzyme human Butyrylcholinesterase (hBChE) will be investigated in the presence or not of salts and as function of high hydrostatic pressure. The exact effects of lyotropic salts on the structure and dynamics of biological systems is a highly debated question, especially their potential to counteract environmental stresses as pressure. Therefore, we would like to study hBChE under various salt conditions on IN5 and IN13 and conduct molecular dynamics simulations in parallel in order to shed light on the effects of salts of the Hofmeister series on enzymes, water and water-ions interactions. Earlier experiments showed that significant effects can be expected for this enzyme.

Experimental Report

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Data Citation

The recommended format for citing this dataset in a research publication is in the following format:

PETERS Judith; CISSE Aline; KOZA Michael Marek; MASSON Patrick; OLLIVIER Jacques and ZELLER Dominik. (2019). The influence of crowding, cosolvents and high pressure on protein dynamics. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-440

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Metadata

Experiment Parameters

  • Environment temperature

    room temperature
  • Experiment res energy

    10 and 100 ueV

Sample Parameters

  • Formula

    • human butyrylcholinesterase + ammonium sulfate
    • juman butyrylcholinesterase + lithium thiocyanate
    • human butyrylcholinesterase