Surface Interaction of Proteins

Abstract

Proteins contain a lot of hydrogen bonds. The rupture of these
hydrogen bonds are responsible for the helix coil transition in
protein leading to the conformational changes having a little variation
of pH and ionic strength. But the situation is different both in
solid state and in the atmosphere of various percentages of water
vapour. Surface interaction of ammonia gas on casein and ovalbumin
has been found to be facilitated by the adsorption of moisture
on these proteins. The ± interaction and proton transfer on the
surface of solid proteins seem to be easier with moist molecules.
Some conformational changes also occur due to the exchange of
hydrogen bond between ammonia and amide linkages in protein
chain. The exchanging capacity decreased considerably in ammonia
than in the vapour of alcohol.