23 December 2013

Biochemistry Thermodynamics: Lesson 7 - Hess's Law and Practice Problem 4

For the process A ↔ B, Keq (AB) is 0.02 at 37°C. For the process B ↔ C, Keq (BC) = 1000 at 37°C.

a. Determine Keq (AC), the equilibrium constant for the overall process A ↔ C, from Keq (AB) and Keq (BC).


b. Determine standard-state free energy changes for all three processes, and use ΔG°(AC) to determine Keq (AC). Make sure that this value agrees with that determined in part a of this problem




From GARRETT/GRISHAM. Biochemistry, 4E. © 2009 Brooks/Cole, a part of Cengage Learning, Inc. Reproduced by permission. www.cengage.com/permissions 



22 December 2013

Biochemistry Thermodynamics: Practice Problem 3

ATP hydrolysis at pH 7.0 is accompanied by release of hydrogen ion to the medium
ATP4- + HO   ↔ ADP3- + HPO­42- + H+

If the ΔG˚’ for this reaction is -30.5 kJ/mol, what is ΔG˚ (that is, the free energy change for the same reaction with all components including H+, at a standard state of 1M)?



From GARRETT/GRISHAM. Biochemistry, 4E. © 2009 Brooks/Cole, a part of Cengage Learning, Inc. Reproduced by permission. www.cengage.com/permissions 


18 December 2013

Biochemistry Thermodynamics: Lesson 6 - The New Standard State


Learn to calculate the standard state for biochemical reactions. This includes adjustments for when hydrogen ions are either consumed or produced at a neutral pH.

12 December 2013

Biochemistry Thermodynamics: Practice Problem 2


The equilibrium constant for A ↔ B is 0.5 at 20C and 10 at 30C. Assuming ΔH˚ is independent of temperature, calculate ΔH˚, ΔG˚ and ΔS˚ at both temperatures.



From GARRETT/GRISHAM. Biochemistry, 4E. © 2009 Brooks/Cole, a part of Cengage Learning, Inc. Reproduced by permission. www.cengage.com/permissions 

Extra Credit: Why must you assume ΔH is independent of temperature?
--Hint: Look at a Van't Hoff plot.





Biochemistry Thermodynamics: Practice Problem 1

Fructose-1-P + H2O   ↔  Fructose + Pi
Was allowed to proceed at 25 degrees C, to equilibrium. The original Concentration of Fructose-1-P was 0.2M, and 6.52 X 10^-5M at equilibrium. Calculate Keq and free energy of hydrolysis.



From GARRETT/GRISHAM. Biochemistry, 4E. © 2009 Brooks/Cole, a part of Cengage Learning, Inc. Reproduced by permission. www.cengage.com/permissions 



Biochemistry Thermodynamics: Lesson 5 - What is Standard State?

Learn what Standard State means for Gibbs Free Energy, How to calculate changes to standard state, and how to determine if a reaction is spontaneous when temperature and equilibrium are adjusted.


 

Biochemistry Thermodynamics: Lesson 4 - Gibbs Free Energy

Learn to calculate the free energy of a reaction. Using this calculation, you can determine if a reaction is spontaneous or if added energy is needed.


 

08 December 2013

Biochemistry Thermodynamics: Lesson 3 - Entropy (2nd and 3rd Law of thermodynamics)

Using the Second Law of Thermodynamics as a starting point we learn to calculate ΔS

Biochemistry Thermodynamics: Lesson 2 - What is Enthalpy (The 1st Law of Thermodynamics)

Using the first law of thermodynamics as a starting point, I try to explain what Enthalpy is and why it's useful in biochemistry


Biochemistry Thermodynamics: Lesson 1 - The three laws

The three laws of thermodynamics related to biochemistry

Enzymes Lesson 8: Bimolecular Enzyme kinetics


Bimolecular Enzyme Kinetics: Single displacement and Double displacement (AKA Ping-Pong)

Enzymes: Lesson 7 - Inhibitors



Introduction to inhibitors and calculations for Competitive inhibitors



Noncompetitive Inhibition and Uncompetitive inhibition

Enzymes: Lesson 6 - Linear Plots (Linweaver-Burk and Hanes-Wolf)

Derive linear plots from the Michaelis-Menton equation

1. Linweaver-Burk



2. Hanes-Wolf

02 December 2013

Enzymes: Lesson 5, Calculating Velocity of Enzyme Reactions (Michaelis-Menton)

Learn to derive the famous Michaelis-Menton equation for Enzyme Kinetics
Learn what that equation means, and how to use it.

Enzymes: Lesson 4, Changing Reaction Rates

Using the Arrhenius Equation to show two ways in which reaction rates can be changed. Namely, by adjusting Temperature or by adding a catalyst (which changes ΔG,Without changing the overall ΔG)


Enzymes: Lesson 3, Review of Rate Reaction Laws

Review of General Chemistry Reaction rate laws in preparation for rate equations for enzymes

Enzymes: Lesson 2, Nomenclature

A brief overview of how enzymes are named, including Enzyme Commission number, cofactors, and coenzymes


Eznymes: Lesson 1, Catalytic Power

Eznymes: Lesson 1
How to calculate Catalytic Power