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Covalent bond
Strong and sharing electrons in a valence shell
Non covalent bonds
Weaker and based on unequal sharing of electrons between nuclei, polar molecules
Intramolecular bonds
Interaction between biomolecules and domains of biomolecules
Non-polar covalent bond
C - H
Polar covalent bonds
Moderately polar bond -
S - H
Polar bond
N - H
O - H
N - C
O - C
Dipole
Partial separation of charge
Electronegativity
H < C = S << N < O
Hydrogen bonds in water
Central water molecule acts as a hydrogen donor to other molecules
Central water molecule acts as a hydrogen acceptor from other molecules
Hydrogen donor examples
N attached to H and O attached to H
Hydrogen acceptors
N not bonded to anything
O not bonded to anything
O double bonded to C
Hydrogen bonds
A type of dipole-dipole interaction and the most common one in biology
Among the strongest of non-covalent interactions: around 30kJ/mole
Only strong if all the 3 atoms aligned
H atom bonded to electronegative atom —— Another electronegative atom with lone pair electrons
Charge-Charge interactions (ion pairs)
Salt bridges
Electrostatic interactions between opposite charge
Stronger than H bond
Extend greater distances
Charge-Charge interactions
Ion pairs buried within the hydrophobic interior of the protein are more stable
Van der Waals forces
Attraction between stable or inducible dipoles
Only works at very short, optimal distance
Weaker than other dipole interactions - large amount of interactions —> stabilising
Hydrophobic interactions
Association of non-polar groups with most energy attributed to exclusion of water (increased entropy)
Strength of hydrophobic interactions
3-10 kJ/mol
Strength of Van der Waals Forces
0.4-4kJ/mol
Strength of Electrostatic interactions
40-200kJ/mol
Strength of H bonds
2-30kJ/mol
Strength of non covalent bonds
Van der Waals Forces
Hydrophobic interactions
H bonds
Electrostatic interactions