Role of hydrophobic and hydrophilic forces in peptide-protein interaction: new advances.
A considerable part of important biological processes is governed by the noncovalent association of peptides and proteins. Various types of intermolecular forces may be involved in the formation of these molecular assemblies. This review gives a brief account of the physicochemical bases of interactive forces, with special emphasis on their impact on various peptide-protein interactions; summarizes the newest biochemical and biophysical methods for the study of such interactions; and discusses the role of various hydrophilic and hydrophobic forces in peptide-protein interactions in various fields of life sciences, such as immunology, enzymology, receptor binding, and toxicology.
Cserháti
T
T
Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest.
Szögyi
M
M
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000502:physiology*; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D013499:Surface Properties
D010455:Peptides; D011506:Proteins