[PO-D2] Poster Session 2

[P2-28] Design of proteins and biopolymers: role of directional interactions and of water.

^○Valentino Bianco¹, Ivan Coluzza² (1.University of Vienna, Austria, 2.CIC biomaGUNE, center for cooperative research in biomaterials, Spain)

The design of a (bio-)polymer is a rational scheme allowing to transfer the one-dimensional information contained in the polymer sequence into the three-dimensional information contained in the polymer folded conformation.
Proteins are an example of designable heteropolymers able to fold in unique target structures. The stability of the native conformation depends on the protein sequence and on the thermodynamic conditions of temperature and pressure.
In our work we use a multiscale approach to investigate how the geometry of the polymer backbone and the properties of the surrounding water affect the selection and the stability of proteins and, more in general, of artificial heteropolymers.
We find that the key actors are: i) the directional interactions along the backbone and ii) the hydrophilic/hydrophobic composition of the surface and core of the folded structure.

References:

V. Bianco, G. Franzese, C. Dellago, I. Coluzza, Phys. Rev. X 7, 021047, 2017.
V. Bianco, N. Pagès-Gelabert, I. Coluzza, G. Franzese, J. Mol. Liq. 245, 129, 2017.
C. Cardelli, V. Bianco, L. Rovigatti, F. Nerattini, L. Tubiana, C. Dellago, I. Coluzza, Sci. Rep. 7, 4986, 2017.
V. Bianco, G. Franzese, Phys. Rev. Lett. 115, 108101, 2015.
V. Bianco, S. Iskrov, G. Franzese, J. Biol. Phys. 38, 27, 2012.