On the basis of many literature measurements, a critical overview is given on essential
noncovalent interactions in synthetic supramolecular complexes, accompanied by analyses …

Biomolecular recognition can be stubborn; changes in the structures of associating
molecules, or the environments in which they associate, often yield compensating changes …

Entropy effects play an important role in drug–target interactions, but the entropic
contribution to ligand-binding affinity is often neglected by end-point binding free energy …

The value of thoroughly understanding the thermodynamics specific to a drug
discovery/design study is well known. Over the past decade, the crucial roles of water …

The rationalization of non‐covalent binding trends is both of fundamental interest and
provides new design concepts for biomimetic molecular systems. Cucurbit [n] urils (CBn) are …

Recent studies on interaction of graphene oxide with proteins and peptides has attracted a
lot of attention in biomedical applications. Hence, fundamental and experimental estimation …

Biomolecular assembly typically exhibits enthalpy–entropy compensation (EEC) behavior
whose molecular origin remains a long-standing puzzle. While water restructuring is …

Bioavailability of food nutrients can be reduced in the presence of antinutrients such as
phytates and tannins. This work aimed to study bovine serum albumin binding to phytic acid …

Water plays a significant role in the binding process between protein and ligand. However,
the thermodynamics of water molecules are often underestimated, or even ignored, in …

Proteins are polyelectrolytes with acidic and basic amino acids Asp, Glu, Arg, Lys, and His,
making up≈ 25% of the residues. The protonation state of residues, cofactors, and ligands …