Issue 13, 2015

Exploring volume, compressibility and hydration changes of folded proteins upon compression

Abstract

Understanding the physical basis of the structure, stability and function of proteins in solution, including extreme environmental conditions, requires knowledge of their temperature and pressure dependent volumetric properties. One physical–chemical property of proteins that is still little understood is their partial molar volume and its dependence on temperature and pressure. We used molecular dynamics simulations of aqueous solutions of a typical monomeric folded protein, staphylococcal nuclease (SNase), to study and analyze the pressure dependence of the apparent volume, Vapp, and its components by the Voronoi–Delaunay method. We show that the strong decrease of Vapp with pressure (βT = 0.95 × 10−5 bar−1, in very good agreement with the experimental value) is essentially due to the compression of the molecular volume, VM, ultimately, of its internal voids, VemptyM. Changes of the intrinsic volume (defined as the Voronoi volume of the molecule), the contribution of the solvent to the apparent volume, and of the contribution of the boundary voids between the protein and the solvent have also been studied and quantified in detail. The pressure dependences of the volumetric characteristics obtained are compared with the temperature dependent behavior of these quantities and with corresponding results for a natively unfolded polypeptide.

Graphical abstract: Exploring volume, compressibility and hydration changes of folded proteins upon compression

Article information

Article type
Paper
Submitted
15 जनवरी 2015
Accepted
06 फरवरी 2015
First published
09 फरवरी 2015

Phys. Chem. Chem. Phys., 2015,17, 8499-8508

Exploring volume, compressibility and hydration changes of folded proteins upon compression

V. P. Voloshin, N. N. Medvedev, N. Smolin, A. Geiger and R. Winter, Phys. Chem. Chem. Phys., 2015, 17, 8499 DOI: 10.1039/C5CP00251F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements