From random Poincar\'e maps to stochastic mixed-mode-oscillation patterns

We quantify the effect of Gaussian white noise on fast--slow dynamical systems with one fast and two slow variables, which display mixed-mode oscillations owing to the presence of a folded-node singularity. The stochastic system can be described by a continuous-space, discrete-time Markov chain, recording the returns of sample paths to a Poincar\'e section. We provide estimates on the kernel of this Markov chain, depending on the system parameters and the noise intensity. These results yield predictions on the observed random mixed-mode oscillation patterns. Our analysis shows that there is an intricate interplay between the number of small-amplitude oscillations and the global return mechanism. In combination with a local saturation phenomenon near the folded node, this interplay can modify the number of small-amplitude oscillations after a large-amplitude oscillation. Finally, sufficient conditions are derived which determine when the noise increases the number of small-amplitude oscillations and when it decreases this number.Comment: 56 pages, 14 figures; revised versio

Open Spinning Strings

We find classical open string solutions in the AdS_5\times S^5/\Zop_2 orientifold with angular momenta along the five-sphere. The energy of these solutions has an expansion in integral powers of $\lambda$ with sigma-model corrections suppressed by inverse powers of $J$ - the total angular momentum. This gives a prediction for the exact anomalous dimensions of operators in the large $N$ limit of an ${\cal N}=2$ $Sp(N)$ Super-Yang-Mills theory with matter. We also find a simple map between open and closed string solutions. This gives a prediction for an all-loop planar relationship between the anomalous dimensions of single-trace and two-quark operators in the dual gauge theory

Mechanisms underlying sequence-independent beta-sheet formation

We investigate the formation of beta-sheet structures in proteins without taking into account specific sequence-dependent hydrophobic interactions. To accomplish this, we introduce a model which explicitly incorporates both solvation effects and the angular dependence (on the protein backbone) of hydrogen bond formation. The thermodynamics of this model is studied by comparing the restricted partition functions obtained by "unfreezing" successively larger segments of the native beta-sheet structure. Our results suggest that solvation dynamics together with the aforementioned angular dependence gives rise to a generic cooperativity in this class of systems; this result explains why pathological aggregates involving beta-sheet cores can form from many different proteins. Our work provides the foundation for the construction of phenomenological models to investigate the competition between native folding and non-specific aggregation.Comment: 20 pages, 5 figures, Revtex4, simulation mpeg movie available at http://www-physics.ucsd.edu/~guochin/Images/sheet1.mp