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. Author manuscript; available in PMC: 2011 Sep 8.
Published in final edited form as: J Am Chem Soc. 2010 Sep 8;132(35):12378–12387. doi: 10.1021/ja103543s

Table 1.

Self-Association Behavior of α/β-peptides 110a as determined by Sedimentation Equilibrium Experiments

Peptide Best-fit Model for the Observed Equilibrium Sedimentation Behaviorb
1 4
2 4
3 (1,3)c
4 (1,4,5)
5 4
6 (1,4,5)
7 4
8 4
9 (1,5)
10 4
a

Except as noted, sedimentation equilibrium data are for 200 μM peptide solutions in 10 mM aqueous sodium acetate, pH 4.6 + 150 mM NaCl, at 25 °C. Data for 1 and 2 are from reference 48 and are included for comparison.

b

See Supporting Information for details. A single number indicates that the best-fit model was for a single species of the following size: 1=monomer, 2=dimer, 3=trimer, etc. Multipe numbers in parentheses indicate that the best-fit model is for multiple species in equilibrium: (1,4,5) indicates a monomer-tetramer-pentamer equilibrium.

c

Data for 3 were collected at 100 μM peptide and in 10 mM sodium acetate, pH 4.6 (no NaCl).