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'Work environment' affects protein properties
Date:7/3/2014

menon. In a crowded lift or on a crowded train, everybody attempts to avoid direct contact with their neighbours and to assume as compact a posture as possible (e.g. by tucking in their arms). According to the excluded volume theory, the principle of mutual repulsion can be applied to proteins in a densely-packed cellular environment. They assume a compact structure. As a rule, their biologically active status is at the same time their most compact status, which is why the excluded volume theory predicts a stabilisation of the biologically active status.

The study demonstrates that there are more factors at work than just mutual repulsion

Deploying various solvent additives, such as biomacromolecules, sugars and salts, the RUB researchers have imitated various cellular conditions and analysed the way they affect the model protein ubiquitin. They demonstrated that the proteins' behaviour is affected by more than just mutual repulsion between protein and solvent additive. In thermodynamic studies, different stabilisation and destabilisation mechanisms were discovered. Contrary to the expected so-called entropic stabilisation based on the excluded volume effect the researchers observed a so-called enthalpic stabilisation of ubiquitin in the presence of macromolecules, sugars and salts. Enthalpic stabilisation is directly correlated to the strengthening of the chemical bonds in the biologically active status and cannot be explained away with the protein's more compact shape being purely volume-based.

Water as mediator between protein and dissolved substances

The researchers attribute the enthalpic stabilisation phenomenon to a water-mediated process: protein and solvent additive do not interact directly, but following a modification of the water properties of the solvent additives' hydration water, the hydrogen bridge bonds in the protein's biologically active status are optimised. The project was financed by the Returnee Programme o
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Contact: Dr. Simon Ebbinghaus
simon.ebbinghaus@rub.de
49-234-322-5533
Ruhr-University Bochum
Source:Eurekalert  

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'Work environment' affects protein properties
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