Table I.

Biophysical Analyses of N-Trimer Mimics Via CD and AUC

Peptide	[θ222 nm] (deg cm2 dmol−1) 25°C	[θ222 nm] (deg cm2 dmol−1) 37°C	[θ222 nm] (deg cm2 dmol−1) 50°C	Mobs/Mcalc 4°C
eboIZN39IQ	−29,400	−27,900	−27,100	3.24
eboIZN39IQ(D3)	−30,400	−29,300	−28,400	3.22
eboIZN21	−25,500	−24,000	−22,900	3.54
eboIZN21(D2)	−24,800	−22,800	−21,800	3.15

CD scans were performed on the same samples of 11.4 µM eboIZN39IQ, 11.1 µM eboIZN39IQ(D3), 18.0 µM eboIZN21 and 25.3 µM eboIZN21(D2) in 50 mM sodium phosphate, pH 5.8, 150 mM NaCl at 25, 37, and 50°C. The peptides were allowed to equilibrate at each temperature for 10 min, after which no change in signal was seen over time. Sedimentation equilibrium analysis was performed on each peptide at three concentrations each (a starting concentration and two twofold dilutions, with typical starting concentrations between 10 and 30 µM) and a minimum of two speeds, but typically three speeds (18,000, 21,000, and 24,000 rpm). Each data set was globally fit to a single ideal species. Each sedimentation equilibrium analysis was performed 2–4 times and averaged for the above table.