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How do enzymes affect reactions?
- Faster Rate
- Milder Conditions
- Greater Specificity
What two features of Subtrate Binding Sites (Enzymes) need to be complimentary?
- Charge (Surface Potentials)
- Holoenzyme - Enzyme + Cofactor (Active)
- Apoenzyme - Enzyme without cofactor (Inactive)
How are enzymatic reactions controlled?
- Vary amt. of enzyme
- Directly control enzyme (with effector)
What types of enzyme modifications affect activity?
- Covalent Binding
- Non-covalent Binding
- Binding at an Effector Site alters binding of a Different ligand at the Functional (Active) Site.
Binding of a Ligand at a Functional Site alters binding of the same ligand at other Functional Sites
Define the Terms,
- Heterotropic - Effectors are different from ligand/subtrate
- Homotropic - Effectors are same as ligand/substrate
Define the terms (with regards to enzyme effectors),
- Increases Substrate binding affinity
- Decreases Substrate binding affinity
What is a Domain?
A structurally independant unit with characteristics of small globular proteins
What is an α+β domain?
An Antiparallel beta sheet
What is a salt bridge? What are the other two similar types of interaction?
- A salt bridge is an electrostatic polypeptide attraction between polar charged residues.
- Ion-Dipole, Dipole-Dipole and Van Der Waals are the other types of interaction
What are Hyrdogen Bonding and Hydrophobic effect ineractions?
- Hydrogen Bonding is between species with acidic and basic character
- Hyrdophobic effect is the interaction of Nonpolar residues with water
What factors can denature proteins?
- Chaotropic Salts
- Certain Water Soluable Organics
Protein Primary Structure
Sequence of residues
Protein Secondary Structure
Local Spatial Conformation of Backbone
Protein Tertiary Structure
Overall 3D arrangement of polypeptide
Quaternary protein structure
Spatial arrangement of subunits in a multisubint protein
Random mutations in well adapted proteins that do not affect function
Evolved or derived from a common ancestor