Introduction to Biochemistry
- Details
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Reaction table
|
|
Substrate conc. |
Substrate conc. |
|
Rate of Reaction |
Rate of Reaction |
Rate of Reaction |
|
|
in tube |
in cuvette |
|
A600nm min-1 |
A600nm min-1 |
A600nm min-1 |
|
|
|
(So) |
(1/So) |
(Vo) |
(Vo) |
(Vo) |
|
Tube |
(mM) |
(mM) |
|
I |
II |
III |
|
A |
10.0ml |
7.5 ml |
0.223 |
0.571 |
0.789 |
0.561 |
|
|
|
|
|
|
|
|
|
B |
2.5 ml |
7.5 ml |
0.250 |
0.507 |
0.348 |
0.412 |
|
|
|
|
|
|
|
|
|
C |
5.0ml |
5.0 ml |
0.149 |
0.296 |
0.253 |
0.267 |
|
|
|
|
|
|
|
|
|
D |
1.0 ml |
9.0 ml |
0.198 |
0.309 |
0.574 |
0.438 |
|
|
|
|
|
|
|
|
|
E |
0.8 ml |
9.2 ml |
0.104 |
0.219 |
0.204 |
0.210 |
|
|
|
|
|
|
|
|
|
F |
1.0 ml |
9.0 ml |
-0.030 |
-0.006 |
-0.010 |
0.015 |
|
|
|
|
|
|
|
|
|
G |
1.0 ml |
9.0 ml |
-0.033 |
0.005 |
-0.010 |
-0.023 |
|
|
|
|
|
|
|
|
Graphical attachments
Tubes A1 A2 A3
Base rate = 0.223 0.347 0.257 for zero seconds in Tubes A1 A2 A3
Tubes B1 B2 B3
Base rate is = 0.250 0.098 0.100 for zero seconds in tubes B1 B2 B3
Tubes C1 C2 C3
Base rate is = 0.149 0.085 0.090 for zero seconds in tubes C1 C2 C3
Tubes D1 D2 D3
Base rate is = 0.198 0.389 0.181 for zero seconds in tubes D1 D2 D3
Tubes E1 E2 E3
Base rate is = 0.104 0.090 0.096 for zero seconds in Tubes E1 E2 E3
Tubes F1 F2 F3
Base rate is =-0.030 -0.032 -0.008 for zero seconds in tubes F1 F2 F3
Tubes G1 G2 G3
Base rate is = -0.033 -0.034 -0.035 for zero seconds in Tubes G1 G2 G3
- Explain the differences between reaction rates, initial velocity and rate constant (10%)
In Michaelis–Menten kinetics, reaction rate refers to the change in concentration per unit time. The standard unit time used is one second. On the other hand, rate constant refers to the rate of reaction when the molar concentration of each reaction is unity. The initial velocity is the reaction rate in the first second of reaction. The concentration keeps changing as reaction continues.
- Explain the concept “activation energy” (Eact, -G≠ ) and the meaning of the Eyring-Polanyi equation (10%)
Eyring-Polanyi equation is mainly used in chemical reactions to show the variance between the rate of reaction and the change in temperature. The equation combines two main theories in chemical reaction- Kinetic theory of gases and statistical thermal dynamics. Two constants are used in this equation; Boltzmann's constant, and Planck's constant. The equation derives a straight-line slope, which helps to come up with entropy of activation.
- Explain the interplay between enthalpy (H) and entropy (S) changes taking place during ligand binding to an enzyme (10%)
Both enthalpy activation and entropy activation are derived from the same slope in Eyring-Polanyi equation. The relationship between these two activations is referred to as the Enthalpy-entropy compensation. The relationship, which is linear free energy relationship, has entropy being derived from enthalpy activation. Ligand binding to an enzyme is one of the chemical reactions used in case study of enthalpy, entropy relationship.
The graph showing the relationship is as below