Erik Lindahl

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Recap • More on structure • Electrostatics & hydrogen bonds • Van der Waals / Lennard-Jones • Interaction strengths • Energy Landscapes • The Boltzmann Distribution • Free Energy and entropy
To sum up last week • Two critical results: • Protein folding is about conformations of long polypeptide chains - how can it find the best structure? • Reaction directions are determined by free energy; G=E-TS. Stable states are G minima.
Page 1: Protein Physics 2012 Lecture 3, Jan
Page 5 and 6: Water Phase Transitions • Systems
Page 7 and 8: Peer challenge Which is true at roo
Page 9 and 10: H-bond ΔG for proteins In vacuo St
Page 11 and 12: Why do some molecules like oil/gas
Page 13 and 14: 9.25 mol/l ΔG liq➝aq =+6.7kcal/m
Page 15 and 16: ΔG? ΔS? ΔH? ΔG= ΔE - TΔS
Page 17 and 18: S vs. Temperature • dF=d(E-TS)=dE
Page 19 and 20: Hydrophobic effect Can you account
Page 21 and 22: Thermodynamic data ∆G virtually p
Page 23 and 24: Amino acid area • For amino acids
Page 27 and 28: What abour proteins? • Folding mo
Page 29 and 30: ΔG of Protein Folding 90% Hydropho
Page 31 and 32: Cost of forming charge • Bring a
Page 33 and 34: Charges in protein • It costs rou
Page 35 and 36: What is ε in a protein?
Page 37 and 38: Superscreening! • Protein surface
Page 39 and 40: Electrostatics on the atomic level
Page 41 and 42: And even closer... ε?
Page 43 and 44: Salt solubility in water Energy bet
Page 45 and 46: Disulphides

Erik Lindahl

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