Hydrogen bonding entropic factors

Several different forces may be involved in protein adsorption at the solid-liquid interface hydrogen bonding, electrostatic forces, and hydrophobic interactions. Entropic factors such as loss of water, structural deformation of the protein onto hydrophobic patches and dehydration of the protein may drive the adsorption process when there are non favourable electrostatic interactions. 

The formation of stable secondary structures and a unique tertiary structure of proteins are dictated by the interactions between constituent amino acid residues along the polypeptide chain and by their interactions with the surrounding medium. During the process of protein folding, the hydrophobic force drives the polypeptide chain to the folded state and overcomes the entropic factors while hydrogen bonds, ion pairs, disulhde bonds, and van der Waals interactions define the shape and keep it from falling apart. The structure of a protein mainly dictates its function, and the attainment of stable conformation is essential for proper function. Hence, many methods have been developed to determine the three-dimensional structures of proteins experimentally. 

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