Toward the development of peptide nanofilaments and nanoropes as smart materials

Wagner et al. 10.1073/pnas.0505871102.

Supporting Information

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Supporting Table 3
Supporting Figure 4




Fig. 4. Analysis of CpA with a deprotected cysteine. (A) Spectra were measured at 25°C by using 150 mM peptide and 10 mM Tris·HCl, pH 8.0 (nonreducing conditions). The (NH4)2SO4 concentrations used were 0.25, 0.50, 0.75, and 1.0 M. (B) Thermal unfolding for CpA with the deprotected cysteine (dashed line) was measured at 150 mM peptide, 0.5 M (NH4)2SO4, and 10 mM Tris·HCl, pH 8.0 (nonreducing conditions). Thermal unfolding of CpA with the Acm-protected cysteine (solid line), taken under the identical conditions, is shown for comparison.





Table 3. Polymerization of CpA with deprotected cysteine

Parameter

1.5 M NaCl

4 M NaCl

0.75 M (NH4)2SO4

s20,w

4.7

9.0

4.9

D20,w

5.6

5.8

3.2

Molecular mass, kDa

81

150

144

No. of monomers

23

41

39

The samples contained 100 mM peptide and 10 mM Tris·HCl, pH 8.0 and were measured at 4°C. s20,w and D20,w are standardized values for pure water at 20°C for both the Svedberg values (in units of 10-13 S) and diffusion constants [in units of cm2 ·s-1 (´10-7)], respectively, as measured by sedimentation velocity experiments (Optima XLA analytical ultracentrifuge, Beckman Instruments). The approximate molecular mass (103 Da) was calculated from the Svedberg values and diffusion constants by using DCDT+. The number of monomers is calculated by dividing the measured molecular mass with the monomer theoretical molecular mass.

This Article

  1. Published online before print August 29, 2005, doi: 10.1073/pnas.0505871102 PNAS September 6, 2005 vol. 102 no. 36 12656-12661
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