Role of Water in the Selection of Stable Proteins at Ambient and Extreme Thermodynamic Conditions

Autor(en)

Valentino Bianco, Giancarlo Franzese, Christoph Dellago, Ivan Coluzza

Abstrakt

Proteins that are functional at ambient conditions do not necessarily work at extreme conditions of temperature T and pressure P. Furthermore, there are limits of T and P above which no protein has a stable functional state. Here, we show that these limits and the selection mechanisms for working proteins depend on how the properties of the surrounding water change with T and P. We find that proteins selected at high T are superstable and are characterized by a nonextreme segregation of a hydrophilic surface and a hydrophobic core. Surprisingly, a larger segregation reduces the stability range in T and P. Our computer simulations, based on a new protein design protocol, explain the hydropathy profile of proteins as a consequence of a selection process influenced by water. Our results, potentially useful for engineering proteins and drugs working far from ambient conditions, offer an alternative rationale to the evolutionary action exerted by the environment in extreme conditions.

Organisation(en)

Computergestützte Physik und Physik der Weichen Materie

Externe Organisation(en)

Universitat de Barcelona

Journal

Physical Review X

Band

7

Anzahl der Seiten

15

ISSN

2160-3308

DOI

https://doi.org/10.1103/PhysRevX.7.021047

Publikationsdatum

06-2017

Peer-reviewed

Ja

ÖFOS 2012

106006 Biophysik, 106002 Biochemie, 103029 Statistische Physik

Schlagwörter

ASJC Scopus Sachgebiete

Allgemeine Physik und Astronomie

Link zum Portal

https://ucrisportal.univie.ac.at/de/publications/27a3c4b3-c04b-4fc8-9b9a-ede10ec0d60e