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Lecture 9

Lecture 9 – Thermodynamics of Protein Folding.docx

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Department
Life Sciences
Course
Life Sciences 1a
Professor
Robert Lue
Semester
Fall

Description
Oct 1 – Thermodynamics of Protein Folding ­ electrostatic forces stabilize protein folding ­ intermolecular bonds ­ side chains hang off peptide backbone ­ hydrogen bonds between amine and carbonyl, dipole­dipole, restrict  conformations, stabilize folded state, backbone interactions  ­ non­polar side chains can have van der Waals interactions , weakest but can be  stronger with large surface area ­ hydrophobic effect  ▯net force not real force ­ real forces made by intermolecular or intramolecular bonds ­ interior of protein composed of hydrophobic, nonpolar side chains ­ non­polar side chains can interact with water (induced dipole­dipole interactions)  but water wants to make stronger bonds to itself or polar side chains  ­ have to add energy to unfold ribonuclease  ­ when ribonuclease is cooled down, it refolds ­ because refolding happens spontaneously without adding energy, delta G of the  unfolded ribonuclease to folded ribonuclease reaction is negative ­ at high temperature, delta G becomes positive  ­ Gibbs free energy: enthalpy reflects stability of bonds (involve bond energy)  ­ entropy in the world is always increasing, creating order costs energy  ­ delta H and delta S independent of temperature ­ ribonuclease example has negative enthalpy and entropy  ­ delta G only temperature dependent when entropy and enthalpy have same sign  ­ ice melting is endothermic process that occurs spontaneously  ­ heat
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