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BIOCHEM ONE - Review
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How do enzymes affect reactions?
Faster Rate
Milder Conditions
Greater Specificity
Regulatable
What two features of Subtrate Binding Sites (Enzymes) need to be complimentary?
Shape
Charge (Surface Potentials)
Define,
Holoenzyme.
Apoenzyme.
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
Define
Allostery
.
Binding at an
Effector
Site
alters binding of a
Different
ligand at the
Functional
(Active)
Site
.
Define
Cooperativity
.
Binding of a Ligand at a
Functional
Site
alters binding of the
same
ligand at
other
Functional
Sites
Define the Terms,
Heterotropic
Homotropic
Heterotropic - Effectors are different from ligand/subtrate
Homotropic - Effectors are same as ligand/substrate
Define the terms (with regards to enzyme effectors),
Activator
Inhibitor
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?
pH
Detergent
Chaotropic Salts
Temperature
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
Neutral Drift
Random mutations in well adapted proteins that do not affect function
Homologous
Evolved or derived from a common ancestor
Author
Ant
ID
241200
Card Set
BIOCHEM ONE - Review
Description
Biochem
Updated
2013-10-18T14:36:32Z
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