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Lecture 11

BIOL 201 Lecture Notes - Lecture 11: 2-Mercaptoethanol, Peptide, Drinking Water Quality Standards

Course Code
BIOL 201
Robin Young

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Review: Protein Folding
Protein Folding is critical for cell function:
In some cases, it appears to be lethal.
Mad cow disease: associated with the aggregation of misfolded proteins that form insoluble
plaques. However, it is not known if these are the cause or just a symptom of the disease.
PrPsc structure: α-helices changed to β-sheets (with hydrophobic phase that binds to other sheets
that have hydrophobic residues – strong interaction)
Thermodynamics of Protein Folding
1. Introduction
- Denaturation
- Spontaneous folding (RNAse Experiment)
2. Terminology and equations
3. The Role of Enthalpy
4. The Role of Entropy
5. The Hydrophobic Effect
Folding Kinetics vs. Thermodynamics
- “Driving force” or “potential” for folding
- Involves comparisons between stability of the unfolded vs. folded state – “are they favorable
to fold?”
- Deals with “why do proteins fold?”
- Tries to address the mechanism (pathway) of folding
- Deals with “how do proteins fold?”
Folding can be thermodynamically favorable and kinetically unfavorable, and vice versa.
Studying Protein Folding
If you want to learn how something works, take it apart (to see what the components are).
Research using protein unfolding has told us a lot about protein folding:
- To what extent can we take a protein apart?
- What is functionally lost?
- After taking it apart, can it be put back together?
- Is the process reversible?
-What can we use to take a protein apart?
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