Role of hydrophobic and hydrophilic forces in peptide-protein interaction

New advances

T. Cserháti, Maria Szögyi

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)165-173
Number of pages9
JournalPeptides
Volume16
Issue number1
DOIs
Publication statusPublished - 1995

Fingerprint

Peptides
Immunology
Biological Phenomena
Proteins
Biological Science Disciplines
Allergy and Immunology
Toxicology

Keywords

  • Hydrophobic and hydrophilic forces
  • Peptide-protein interactions

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Role of hydrophobic and hydrophilic forces in peptide-protein interaction : New advances. / Cserháti, T.; Szögyi, Maria.

In: Peptides, Vol. 16, No. 1, 1995, p. 165-173.

Research output: Contribution to journalArticle

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