Universal Scaling of Cavity Volume Pathways in Globular Proteins

Universal behavior of localization of residue fluctuations in globular proteins.

Localization properties of residue fluctuations in globular proteins are studied theoretically by using a Gaussian network model. Participation ratio for each residue fluctuation mode is calculated. It is found that the relationship between participation ratio and frequency is similar for all globular proteins, indicating a universal behavior in spite of their different size, shape, and archite...

Native topology determines force-induced unfolding pathways in globular proteins.

Single-molecule manipulation techniques reveal that stretching unravels individually folded domains in the muscle protein titin and the extracellular matrix protein tenascin. These elastic proteins contain tandem repeats of folded domains with beta-sandwich architecture. Herein, we propose by stretching two model sequences (S1 and S2) with four-stranded beta-barrel topology that unfolding force...

Volume Determination of Globular Proteins by Molecular Dynamics

Molecular dynamics simulations of myoglobin and aspartate aminotransferase, with explicit solvent, are shown to accurately reproduce the experimentally measured molar volumes. Single aminoacid substitution at VAL39 of aspartate aminotransferase is known to produce large volumetric changes in the enzyme, and this effect is demonstrated in simulation as well. This molecular dynamics approach, whi...

Beyond Scaling Up: Pathways to Universal Access to Health Services

Universal scalings of universal scaling exponents

In the last decades, renormalization group (RG) ideas have been applied to describe universal properties of different routes to chaos (quasi-periodic, period doubling or tripling, Siegel disk boundaries, etc.). Each of the RG theories leads to universal scaling exponents which are related to the action of certain RG operators. The goal of this announcement is to show that there is a principle t...