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Interaction of soluble proteins with protein monolayers
Author(s) -
Arnold John D.,
Pak Charles Y.
Publication year - 1968
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02915336
Subject(s) - solubility , monolayer , intermolecular force , protein tertiary structure , chemistry , water soluble , aqueous solution , protein structure , biophysics , protein secondary structure , molecule , phase (matter) , chemical physics , crystallography , chemical engineering , biochemistry , organic chemistry , biology , engineering
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.