1What are the circled called bonds called and what are their purpose?

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.
2Describe how peptide bonds are formed?
Peptide bonds are formed from Carboxy ends connecting to the N terminus end from both Amino Acids.
3Why do proteins fold?
- Intramolecular forces, such as hydrogen bonds, ionic bonds, van der Waals.
- Polarity
- Distribution of Amino Acids
4Describe how nonpolar and polar amino acids arrange/cluster in a molecule?
Nonpolar Amino Acids cluster in the interior of a peptide and Polar Amino Acids are arranged on the outside of the molecule.
5Molecular Chaperones
Binds to partly folded proteins and helps them progress along the more energy-efficient folding pathway.
6Describe all protein levels of organization:
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.
7Where are Alpha Helices found?
In transport proteins and receptors. Flexible and Fibrous alpha helices.
8What are the 2 ways Beta sheets can be formed?
From a parallel polypeptide running in same direction called parallel chains, a polypeptide chain that folds back and forth upon itself called antiparallel chains.
9What are Beta Barrels?
Very large beta sheet that curves on itself, acts as water channels (porins).
10What is protein function dependent on?
Shape
11What are the different methods that proteins bind to other proteins?
Surface to surface interaction, Surface to string interaction, Coiled coil interaction or helix helix.

12Describe protein binding
Protein binding is specific, substance bound to the protein is a ligand and depends on high affinity and formation of noncovalent bonds.
13Define the Vmax

The max rate of product being produced in a reaction
14Define the Km

Half of the Vmax
15How do you reach Vmax?

Increasing Substrate concentration.
16Enzymes have a higher affinity for _____ state than the _____ "_____" stable state
Transition, Basic normal
17Define Positive Feedback
Where allosteric binding of a ligand actualy increases activity of enzyme.
18What does GTP do for a reaction?
Increases or activates activity.
19Describe Competitive, Noncompetitive and Uncompetitive inhibition:

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