Bonding Flashcards
Bonding
Electronegativity is a measure of the degree to which an atom draws electrons towards itself.
Polar covalent bond is distorted in equal distribution
Bonding
Atoms share electrons in covalent bonds in order that attains a full outer electron energy.greater stability.
Covalent bonded atoms can rotate freely about a sigma molecular orbital
Summing up
Covalent bonds formed sharing 2 e between 2 atoms
Coordinate formed where both e in bond provide 1 of atoms
Peptide bond
Proteins are polymers of aa
Between the carboxyl group
Causes condensation reaction
Hybridisation of atomic orbitals have same energy level
Cont
Max the number of covalent bonds Stable the atom 3 of 4 orbitals hybridise Form sigma bonds E move between p orbitals
Cont
Peptide bond has a partial double bond character Rigid if peptide bond Reduces freedom if folding Double bond character 6 atoms involved
Cont
Peptide bond is invariably found in the trans confirmation
Donation of electrons
Atom make the carbonyl less elextrophiillic
Cont
Special amino acid proline Unusual in amino group Proline forms peptide bonds Ring structure Lacks a parietal double bond Rotation in peptide bond
Interactions between molecules
Molecules must interact bind Initiate an action Enzyme binding to its substrate Hormone binding to its receptor RNA being transcribed on DNA template
Cont
Regnition Intermolecular interactions Known as electrostatic or hydrophobic in nature Classify as hydrogen bonding Short range
Hydrogen bonding
Occurs between water molecules
Electronegative oxygen draws electrons
Slight pos charge
Has two lone pairs
Cont
Strong electronegative atom There is an acceptor There is a donor Has special characteristics The bond would be aligned
Cont
Distances and orientations Optimum length Occur between purine and pryrinidibe base I opposite DNA Genetic code
Charge charge interactions
Electrostatic in nature
Distances between interacting groups not fixed
Acidic or basic group
Has a lone pair of electrons
Cont
Interaction may be attractive or repulsive
Charge at physiological ph
Protein has aa
Long peptide chains
Interaction between charged groups ph dependant