In: Anatomy and Physiology
What happens in a hydrophobic interaction between R groups to give a protein is shape?
For R groups to form ionic bond what types of molecules must be present?
Please explain so I can understand
There are hydrophilic aminoacids and hydropohobic aminoacids.Hydrophilic amino acids are those aminoacids which are polar.Hydrophobic aminoacids are the Aminoacids that contain Non Polar R group which are Hydrophobic.
The Hydrophilic aminoacids can dissolve in water,so they can join with hydrogen bond network formed by polar water.
The Hydrophobic Interactions in the non polar aminoacids with non polar side side chains are important in the tertiary structure of a protein.These hydrophobic molecules cluster on inside of the Protein ,leaving the hydrophilic aminoacids outside to Interact with surrounding water molecules .
When These cluster of Hydrophobic R group are surrounding the water molecule,it destabilize the Protein and make it water insoluble.So the protein moleculse reshape themselves in ways so that this couldnot happen.so protiens have their hydrophobic R-groups buried within their core, so that a water excluding region is formed that plays a important role in maintaining the overall3D structure of the final protein molecule.
Ionic bond is formed by the transfer of Valence Electrons.so that a positive charged ion(molecule that loses electron) and a negative charged ion(molecule that gain electrons) are formed.CHarged amino acids can form Ionic Bond
(Polar Aminoacids form Hydrogen Bond and Non polar amino acid from hydrophobic interactions)
The presence of Functional Group Carboxyl can make Aminoacids form Ionic Bond.The carboxyl group ,In its protonated state can form hydrogen bonds But In its deprotonated states, it form ionic bonds with other +ve charged compounds.
Examples of Aminoacids that form Ionic bonds are- Aspartate, Histidine, Glutamate, Arginine