Interaction of soluble proteins with protein monolayers

John D. Arnold, Charles Y. Pak

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The direction and strength of intermolecular forces at an air-water or oil-water interface is such that many proteins in the interface are distorted in structure. This involves substantial changes in solubility and cross-sectional area. Many of the changes can be accounted for by rupture of the secondary and tertiary bonds and are often irreversible. The hydrophilic groups of the protein will be concentrated in the aqueous phase and participate in interactions with normal proteins in the supporting solution. It can be shown that certain types of interaction between these hydrophilic groups of a protein monofilm and a soluble protein are dependent on the interfacial pressure, that they are sensitive to a small (one or more amino acid) change in structure of the protein. Evidence is given that they are related to certain antigen-antibody type reactions between molecules in three-dimensional systems. Since many proteins in vivo are exposed to oilwater and air-water interfaces, this laboratory model may have physiologic as well as chemical significance.

Original languageEnglish (US)
Pages (from-to)128-138
Number of pages11
JournalJournal of the American Oil Chemists Society
Volume45
Issue number3
DOIs
StatePublished - Mar 1968

Fingerprint

Monolayers
Proteins
proteins
Water
oil-water interface
Air
air
Antigen-Antibody Reactions
water
protein structure
strength (mechanics)
Antigens
solubility
Hydrophobic and Hydrophilic Interactions
Antibodies
Solubility
Amino acids
Rupture
Oils
antigens

ASJC Scopus subject areas

  • Organic Chemistry
  • Chemical Engineering(all)
  • Food Science
  • Chemistry (miscellaneous)

Cite this

Interaction of soluble proteins with protein monolayers. / Arnold, John D.; Pak, Charles Y.

In: Journal of the American Oil Chemists Society, Vol. 45, No. 3, 03.1968, p. 128-138.

Research output: Contribution to journalArticle

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