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Our main focus is on how fundamental physical forces drive molecular processes and how they are related to particular phenomena like protein folding, hydrophobic effect, formation of ligand-receptor complexes, self-assembly of peptides, protein-membrane interaction, reaction kinetics, etc.
Understanding intra and intermolecular non-covalent interactions (hydrophobicity, hydrogen bonding, electrostatics, solvation, intrinsic conformational preferences of amino acid residues, protein nearest-neighbor effect, van der Waals interactions, salt bridges, etc.) is crucial for developing detailed and quantitative descriptions of biomolecular processes. Energetics and nature of molecular interactions in biomolecules is a highly controversial issue. Since many biomolecules (proteins, protein complexes, DNA, membranes) are only weakly stable at room temperature, all types of molecular interactions are important. For example, intrinsic conformational preferences of amino acid residues provide only a few tenths of kcal/(mol-per-residues) to stability of the folded state; however, they are essential in folding a protein from unfolded state to the correct biologically active conformation. Our findings suggest that electrostatic screening i.e. environment dependent balance between electrostatic interactions and solvation, is the crucial mechanism in determining nature and energetics of hydrophobicity, conformational preferences, and the nearest-neighbor effect.

Conformational preferences of amino acid residues and nearest-neighbor effect

Origin of hydrophobicity

Ligand-receptor interactions

Mechanistic view of biological function

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