Surface Interaction of Proteins

摘要

Proteins contain a lot of hydrogen bonds. The rupute of these hydrogen bonds are responsible for the helix coil transition in protein leading to conformational changes having a little variation of PH and ionic strength. But the situation is different both in solid state and interaction of ammonia gas on casein and ovalbumin has proteins. The +- interaction and prton transfer on the surface of solid proteins seem to be easier with mosit molecules. Some conformational changes also occur due to te exchange of hydrogen bond between ammonia and amide linkages in protein chain. The exchanging capacity decreased condiderably in ammonia than in the vapour of alcohol