Unformatted text preview: What visual model best displays a protein’s secondary structures ( helices and α sheets)? β (a) ribbon (b) space-filling (c) backbone (d) wire 3 Typical folded proteins have a stability ranging from 7 to 15 kcal/mol at 37°C. Stability is a measure of the equilibrium between the folded (F) and unfolded (U) forms of the protein, with the unfolded form having a greater free energy. See Figure Q4-10: for a protein with a stability of 7.1 kcal/mol, calculate the fraction of protein that would be unfolded at equilibrium at 37°C. The equilibrium constant ( K eq ) is related to the free energy (D G °) by the equation K eq = 10 –D G °/1.42 . Figure Q4-10...
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- Summer '12
- tissues. Unfolded proteins, different target protein