Biochem Office hours exam 1
Overview of Lecture Concepts
Contextual Applications of TKA:
TKA (theoretical knowledge application) is applied in scenarios like
Ion Exchange Chromatography: Understanding movement based on charge (positive/negative).
Direct pKa Questions: Can be quantitative and qualitative.
Relevant in experiments such as chromatography, emphasizing practical implications of these theories.
General Understanding of pKa and Pi
pKa: Influences the isoelectric point (pI), which is critical for understanding protein behavior.
Isoelectric Focusing: Involves the concept of pI and its relation to pKa.
Summary of Lecture Six
Protein Dynamics:
Essential in cellular processes as they dictate actions in biochemical reactions.
Kinetics:
Driven by energy, differentiating between endergonic (energy input required) vs exergonic (energy released) reactions.
Analogous to logistics in planning—having the energy doesn't guarantee execution.
Kinetics Fundamentals
Velocity of Reaction:
Defined as the change in concentration of reactants/products over time.
Influencing Factors:
Concentration of reactants and probability of interaction.
Rate Constant (k):
A critical variable summarizing multiple kinetic factors.
Equilibrium (KEQ):
Equal velocities in forward and reverse reactions; affected by rate constants.
Kinetic Theory
Statistical Nature of Biochemistry:
Biochemical changes indicate likelihood rather than certainties.
Key Variables:
Temperature and Activation Energy (Ea):
Ea: Minimum energy needed for the reaction to occur.
Temperature: Relates to kinetic energy of molecules.
Enzyme Kinetics
Role of Enzymes in Velocity:
Enzymes speed up reactions without altering the change in Gibbs Free Energy (ΔG).
The enzyme's role reduces the energy barrier between reactants and the transition state.
Orders of Reaction:
Zero Order: Reaction rate independent of reactant concentration
First Order: Rate depends on the concentration of one reactant.
Second Order: Rate depends on concentrations of two reactants simultaneously.
Michaelis-Menten Kinetics
Michaelis Constant (Km):
Reflects affinity between enzyme and substrate; Lower Km indicates higher affinity.
Kcat:
Represents turnover number of the enzyme, linking enzymatic performance to chemical steps.
Catalytic Efficiency:
Ideally, enzymes should have high catalytic efficiency optimized for reaction specificity.
Exam Preparation
Practical Application:
Expect to use the Michaelis-Menten equation for calculations in research contexts.
Review Focus:
Emphasis on understanding concepts over intensive math; basic algebra applicable.
Expect multiple-choice format; familiarize with equations and contextual applications.
Lecture Materials and Resources
Suggested videos and channels for additional learning:
AK Lectures
Orgo Chem Tutor
Final Thoughts
Explaining Concepts:
Clear understanding is emphasized over rote memorization of equations.
Focus on how various thermodynamic principles tie into protein folding and behavior.