The functions of many proteins are regulated through allostery, whereby effector binding at a
distal site changes the functional activity (eg, substrate binding affinity or catalytic efficiency) …

Energy flows anisotropically through the residues and vibrational states of globular proteins.
A variety of experimental and computational studies have identified energy transport …

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The three-dimensional structure of a protein is formed and maintained by the noncovalent
interactions among the amino-acid residues of the polypeptide chain. These interactions can …

Linking cell signaling events to the fundamental physicochemical basis of the
conformational behavior of single molecules and ultimately to cellular function is a key …

Highlights•Advances in computational methods for allosteric pathways are reviewed.•New
methods are able to replicate many but not all experimental results.•Each method accesses …

Molecular dynamics (MD) simulations have become a powerful and popular method for the
study of protein allostery, the widespread phenomenon in which a stimulus at one site on a …

We review a theory for coupled many-nonlinear oscillator systems that describes quantum
ergodicity and energy flow in molecules. The theory exploits the isomorphism between …

Allosteric effect implies ligand binding at one site leading to structural and/or dynamical
changes at a distant site. PDZ domains are classic examples of dynamic allostery without …

Energy landscape theories have provided a common ground for understanding the protein
folding problem, which once seemed to be overwhelmingly complicated. At the same time …