Membrane proteins are essential for the survival of living organisms. They involved in important biological functions including transportation ions and molecules across cell membrane triggering signaling pathways. targets more than half modern medical drugs. Despite their significance, information about structural dynamics is lagging when compared to that globular proteins. The major challenges...

The solvent-excluded volume effect is an under-appreciated general phenomenon occurring in liquids and playing a fundamental role many cases. It quantified characterized by means of the theoretical concept cavity creation its Gibbs free energy cost. magnitude reversible work proves to be particularly large water, this fact plays key for, among other things, poor solubility nonpolar species, for...

Hydration water is vital for various macromolecular biological activities, such as specific ligand recognition, enzyme activity, response to receptor binding, and energy transduction. Without hydration water, proteins would not fold correctly and would lack the conformational flexibility that animates their three-dimensional structures. Motions in globular, soluble proteins are thought to be go...

We consider a nonstatistical, computationally fast experiment to identify important topological constraints in folding small globular proteins of about 100-200 amino acids. In this experiment, proteins are expanded mechanically along a path of steepest increase in the free space around residues. The pathways are often consistent with folding scenarios reported in kinetics experiments and most a...

Extent of binding (gammap) of globular proteins to calf-thymus DNA have been measured in mole per mole of nucleotide as function of equilibrium protein concentration. We have exploited measurement of the surface tension of the protein solution in the presence and absence of DNA to calculate the binding ration (gammap). Interaction of bovine serum albumin with DNA has been studied at different p...

It is known that larger globular proteins are built from domains, relatively independent structural units. A domain size seems to be limited, and a single domain consists of from few tens to a couple of hundred amino acids. Based on Monte Carlo simulations of a reduced protein model restricted to the face centered simple cubic lattice, with a minimal set of short-range and long-range interactio...

Intrinsically Disordered Proteins and Regions (IDPs/IDRs) are key components of a multitude biological processes. Conformational malleability enables IDPs/IDRs to perform very specialized functions that cannot be accomplished by globular proteins. The functional role for most these proteins is related the recognition other biomolecules regulate processes or as part signaling pathways. Depending...

The influence of hydration on the internal dynamics of a typical EF-hand calciprotein, parvalbumin, was investigated by incoherent quasi-elastic neutron scattering (IQNS) and solid-state 13C-NMR spectroscopy using the powdered protein at different hydration levels. Both approaches establish an increase in protein dynamics upon progressive hydration above a threshold that only corresponds to par...

The phase behavior of protein solutions is important for numerous phenomena in biology and soft matter. We report a lower critical solution temperature (LCST) phase behavior of aqueous solutions of a globular protein induced by multivalent metal ions around physiological temperatures. The LCST behavior manifests itself via a liquid-liquid phase separation of the protein-salt solution upon heati...

Sso7d from the thermoacidophilic archaebacterium Sulfolobus solfataricus is a small globular protein with a known three-dimensional structure. Inspection of the structure reveals that Phe31 is a member of the aromatic cluster forming the protein hydrophobic core, whereas Trp23 is located on the protein surface and its side chain exposed to the solvent. The thermodynamic consequences of the subs...