1st talk:

Applications of Multiferroics: from elementary-particle physics to future nanodevices

Speaker:

Dr. Marjana Lezaic, PGI-1/IAS-1

Contents:

Multiferroic materials, possessing both ferroelectric and ferromagnetic order in the same phase, are currently one of the spots of high interest in solid-state investigations.

We use first-principles calculations to demonstrate a possible way to employ multiferroic materials in nanodevices where the magnetization direction is controlled with an external electric field; in contrast to this application which should eventually take place at room temperature, we show that multiferroics can also be used in experiments conducted at liquid helium temperature, searching for the permanent electric dipole moment of electron.

2nd talk:

New developments in the Lund protein folding model

Speaker:

Dr. Sandipan Mohanty, JSC

Contents:

The Lund protein folding model is a physics based implicit solvent all-atom protein model aiming to provide a good approximate description of large scale conformational changes in proteins, such as folding and aggregation. It was developed through high statistics Monte Carlo folding simulations of a number of small peptides with alpha-helix and beta-strand secondary structure. Previously it has been shown that this model describes the folding and thermodynamic behaviour of a set of 17 small peptides and the folding properties of 3 small protein systems of 49-67 residues. The model has also been used for studies of aggregation of A beta_16-22 , A beta_25-35 and Ac-PHF6-NH2 peptides, as well as thermal and mechanical unfolding of ubiquitin. In this presentation, I will briefly summarise our recent work in connection with this force field and simulation techniques, with the long term goal of being able to simulate average sized protein domains. In particular, I will discuss in detail a computational study of the folding and thermodynamic behaviour of a new 73 residue 3-helix bundle protein. I will conclude with some exciting preliminary results from an ongoing study, in which a 92 residue mixed alpha/beta protein with a complex topology folds reproducibly in our unbiased all-atom simulations, starting from random initial conformations.