Angel E. Garcia

TL;DR: A molecular-dynamics calculation on a hydrated protein, crambin, demonstrates that neighboring dihedral angles are correlated to local transitions in the protein backbone, and that the amplitude of collective excitations, representing correlated global motions in theprotein, samples multicentered distributions.

TL;DR: In this paper, the hydration free energies of ions exhibit an approximately quadratic dependence on the ionic charge, as predicted by the Born model, and the average and fluctuation of the electrostatic potential at charge sites appear as the first coefficients in a Taylor expansion of the free energy of charging.

TL;DR: A review of the experimental and computational advances over the past decade in understanding the role of water in the dynamics, structure, and function of proteins focuses on the combination of X-ray and neutron crystallography, NMR, terahertz spectroscopy, mass spectroscopic, thermodynamics, and computer simulations to reveal how water assist proteins in their function.

TL;DR: The pressure denaturation puzzle is resolved by focusing on the pressure-dependent transfer of water into the protein interior, in contrast to the transfer of nonpolar residues into water, the approach commonly taken in models of protein unfolding.

TL;DR: This model is shown to account quantitatively for the central hydrophobic phenomena of cavity formation and association of inert gas solutes and the simplicity and flexibility of the approach suggest that it should permit applications to conformational equilibria of nonpolar solute andhydrophobic residues in biopolymers.