Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation.

The diffusion coefficients of globular and fully unfolded proteins can be predicted with high accuracy solely from their mass or chain length. However, this approach fails for intrinsically disordered proteins (IDPs) containing structural domains. We propose a rapid predictive methodology for estimating the diffusion coefficients of IDPs.

Diversity of hydrodynamic radii of intrinsically disordered proteins.

Intrinsically disordered proteins (IDPs) form an important class of biomolecules regulating biological processes in higher organisms. The lack of a fixed spatial structure facilitates them to perform their regulatory functions and allows the efficiency of biochemical reactions to be controlled by temperature and the cellular environment. From the biophysical point of view, IDPs are biopolymers with a broad configuration state space and their actual conformation depends on non-covalent interactions of its amino acid side chain groups at given temperature and chemical conditions.

Variability in melatonin concentration in blood serum of patients with episodic migraine: a pilot study.

Aim Of Study: This study was aimed at assessing the possible effect of melatonin concentration on migraine. The serum concentration profile of melatonin in patients with diagnosed episodic migraine in the interictal period was compared to the profile in patients without migraine. Then, a correlation between the frequency and duration of migraine attacks, and the possible relationship between these parameters and melatonin levels in individual patients, was established.