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Using lattice models we explore the factors that determine the tendencies of polypeptide chains to aggregate by exhaustively sampling the sequence and conformational space. The morphologies of the fibril-like structures and the time scales ($tau_{fib}$) for their formation depend on a balance between hydrophobic and coulomb interactions. The extent of population of an ensemble of textbf{N$^*$} structures, which are fibril-prone structures in the spectrum of conformations of an isolated protein, is the major determinant of $tau_{fib}$. This observation is used to determine the aggregating sequences by exhaustively exploring the sequence space, thus providing a basis for genome wide search of fragments that are aggregation prone.
Using lattice models we explore the factors that determine the tendencies of polypeptide chains to aggregate by exhaustively sampling the sequence and conformational space. The morphologies of the fibril-like structures and the time scales ($tau_{fib
We present results of molecular simulations of a model protein whose hydrophobic collapse proceeds as a cascade of downhill transitions between distinct intermediate states. Different intermediates are stabilized by means of appropriate harmonic cons
We consider the unwinding of two lattice polymer strands of length N that are initially wound around each other in a double-helical conformation and evolve through Rouse dynamics. The problem relates to quickly bringing a double-stranded polymer well
We present a comparison between Fe K-edge x-ray absorption spectra of carbonmonoxy-myoglobin and its simulation based on density-functional theory determination of the structure and vibrations and spectral simulation with multiple-scattering theory.
In this paper we explore relevant electrical properties of two olfactory receptors (ORs), one from rat OR I7 and the other from human OR 17-40, which are of interest for the realization of smell nanobiosensors. The investigation compares existing exp