Proteins and Enzymes

Psi bond is C-C and Phi bond is C-N, they allow rotation of the sides of the polypeptide backbone to fit into position of lowest free energy.

Peptide bonds are formed from Carboxy ends connecting to the N terminus end from both Amino Acids.

- Intramolecular forces, such as hydrogen bonds, ionic bonds, van der Waals.
- Polarity
- Distribution of Amino Acids

Nonpolar Amino Acids cluster in the interior of a peptide and Polar Amino Acids are arranged on the outside of the molecule.

Binds to partly folded proteins and helps them progress along the more energy-efficient folding pathway.

Primary structure - Refers to the Amino Acid sequence
Secondary structure - Segments of the polypeptide sequence that spontaneously form alpha helices and beta sheets. Does not involve R groups. Involves N-H and C=O bonds.
Tertiary structure - Involves R groups, 3D organization that includes all non covalent bonds.
Quaternary structure - Protein has multiple subunits, noncovalent bonds hold the subunits together.

In transport proteins and receptors. Flexible and Fibrous alpha helices.

From a parallel polypeptide running in same direction called parallel chains, a polypeptide chain that folds back and forth upon itself called antiparallel chains.

Very large beta sheet that curves on itself, acts as water channels (porins).

Shape

Surface to surface interaction, Surface to string interaction, Coiled coil interaction or helix helix.

Protein binding is specific, substance bound to the protein is a ligand and depends on high affinity and formation of noncovalent bonds.

The max rate of product being produced in a reaction

Half of the Vmax

Increasing Substrate concentration.

Transition, Basic normal

Where allosteric binding of a ligand actualy increases activity of enzyme.

Increases or activates activity.

Competitive - Vmax same, Km increases
Noncompetitive - Vmax decreases, Km same
Uncompetitive - Vmax decreases, Km decreases