Georgia Institute of Technology College of Sciences

Choose a graph uniformly at random from all d-regular graphs on n vertices. We determine the chromatic number of the graph for about half of all values of d, asymptotically almost surely (a.a.s.) as n grows large. Letting k be the smallest integer satisfying d < 2(k-1)\log(k-1), we show that a random d-regular graph is k-colorable a.a.s. Together with previous results of Molloy and Reed, this establishes the chromatic number as a.a.s. k-1 or k. If furthermore d>(2k-3)\log(k-1) then the chromatic number is a.a.s. k. This is an improvement upon results recently announced by Achlioptas and Moore. The method used is "small subgraph conditioning'' of Robinson and Wormald, applied to count colorings where all color classes have the same size. It is the first rigorously proved result about the chromatic number of random graphs that was proved by small subgraph conditioning. This is joint work with Xavier Perez-Gimenez and Nick Wormald.

A new estimate on weak solutions of the Navier-Stokes equations in three dimensions gives some information about the partial regularity of solutions. In particular, if energy concentration takes place, the dimension of the microlocal singular set cannot be too small. This estimate has a dynamical systems proof. These results are joint work with M. Arnold and A. Biryuk.

We will survey some old, some new, and some open problems in the area of efficient sampling. We will focus on sampling combinatorial structures (such as perfect matchings and independent sets) on regular lattices. These problems arise in statistical physics, where sampling objects on lattices can be used to determine many thermodynamic properties of simple physical systems. For example, perfect matchings on the Cartesian lattice, more commonly referred to as domino tilings of the chessboard, correspond to systems of diatomic molecules. But most importantly they are just cool problems with some beautiful solutions and a surprising number of unsolved challenges!

The stress condition calls for an adequate activity of key enzymatic systems of cellular defense. Massive protein destabilization and degradation is occurring in stressed cells. The rate of protein re-synthesis (DNA->RNA->protein) is inadequate to adapt to rapidly changing environment. Therefore, an alternative mechanism should exist maintaining sufficient activity of defense enzymes. Interestingly, more than 50% of enzymes consist of identical subunits which are forming multimeric interface. Stabilization of multimers is important for enzymatic activity. We found that it can be achieved by the formation of inter-subunit covalent bridges in response to stress conditions. It shows an elegance of the structure design that directs selective subunits linkage and increases enzyme's robustness and chances of cell survival during the stress. In contrast, modification of aminoacids involved in linkage leads to protein destabilization, unfolding and degradation. These results describe a new instantaneous mechanism of structural adaptation that controls enzymatic system under stress condition.