What will happen if some of the hydrogen bonding capable groups such as C=O, O-H or N-H do not form hydrogen bonds in the folded protein?
There are number of interactions which are there to stabilize the folded structure of proteins. One of the most important one is H bonding .
When some of the hydrogen bonds are not there in the folded protein , it tends to destabilize the protein and favours the unfolding of the protein structure.
It plays an important role because it is H bonding which stabilize the secondary , tertiary and quatnary structure of protein and the core of most protein is composed of secondary structure ie alpha helix and beta sheets.
So basically it is the central feature for the stability of protein molecules.
Get Answers For Free
Most questions answered within 1 hours.