BIOL2600 ENZYMES EXAM QUESTIONS AND ANSWERS WITH
COMPLETE SOLUTIONS VERIFIED
Conditions for measuring ΔG°
1. 1M concentration
2. 7pH
3. 298K
4. P = 1atm
Characteristics of a reaction in equilibrium
Forward and backward reaction proceed at the same rate
equilibrium constant expression
Formula for ΔG
ΔG=ΔG°+RT*ln(Q)
How do we know system is in an equilibrium?
ΔG=0
Q vs K
Q is reaction quotient, is uses concentrations at any given point in the reaction, K only
uses equilibrium values.
How is ΔG useful in biochemistry?
It can be used to couple thermodynamically favorable and unfavorable reactions to
make a reaction that is favorable overall
How are protein backbones linked?
, Via amide/peptide bonds
Types of noncovalent bonds in proteins
1. Hydrogen bonds
2. Electrostatic attraction
3. Van der Waals forces
Noncovalent bonds are weaker than covalent bonds, why are they important
Together they are strong
What is protein folding driven by?
formation of hydrophobic core
4 levels of protein structure
1. Primary
2. Secondary
3. Tertiary
4. Quaternary
What does secondary protein structure consist of?
Alpha helices and beta sheets
protein domain
A discrete part of a protein that provides a unit of function
Hemoglobin structure
Tetrameric protein with two alpha chains and two beta chains
Dimer of alpha-beta protomers
Major methods of determining protein structure
COMPLETE SOLUTIONS VERIFIED
Conditions for measuring ΔG°
1. 1M concentration
2. 7pH
3. 298K
4. P = 1atm
Characteristics of a reaction in equilibrium
Forward and backward reaction proceed at the same rate
equilibrium constant expression
Formula for ΔG
ΔG=ΔG°+RT*ln(Q)
How do we know system is in an equilibrium?
ΔG=0
Q vs K
Q is reaction quotient, is uses concentrations at any given point in the reaction, K only
uses equilibrium values.
How is ΔG useful in biochemistry?
It can be used to couple thermodynamically favorable and unfavorable reactions to
make a reaction that is favorable overall
How are protein backbones linked?
, Via amide/peptide bonds
Types of noncovalent bonds in proteins
1. Hydrogen bonds
2. Electrostatic attraction
3. Van der Waals forces
Noncovalent bonds are weaker than covalent bonds, why are they important
Together they are strong
What is protein folding driven by?
formation of hydrophobic core
4 levels of protein structure
1. Primary
2. Secondary
3. Tertiary
4. Quaternary
What does secondary protein structure consist of?
Alpha helices and beta sheets
protein domain
A discrete part of a protein that provides a unit of function
Hemoglobin structure
Tetrameric protein with two alpha chains and two beta chains
Dimer of alpha-beta protomers
Major methods of determining protein structure
