Non-bonding Forces Influencing Protein Structures Amino acids of a protein are joined by covalent bonding interactions.The polypeptide is folded in three dimension by non-bonding interactions.These interactions can easily be disrupted by extreme pH,temperature,denaturants,reducing reagents.We will discuss the nature of these types of forces H-bond interactions(12-30 kJ/mol) Hydrophobic Interactions(<40 kJ/mol) Electrostatic Interactions(20 kJ/mol) Van Der Waals Interactions(0.4-4 kJ/mol) The total inter-atomic force acting between two atoms is the sum of all the forces they exert on each other.Non-bonding Forces Influencing Protein Structures Amino acids of a protein are joined by covalent bonding interactions. The polypeptide is folded in three dimension by non-bonding interactions. These interactions can easily be disrupted by extreme pH, temperature, denaturants, reducing reagents. We will discuss the nature of these types of forces H-bond interactions (12-30 kJ/mol) Hydrophobic Interactions (<40 kJ/mol) Electrostatic Interactions (20 kJ/mol) Van Der Waals Interactions (0.4-4 kJ/mol) The total inter-atomic force acting between two atoms is the sum of all the forces they exert on each other