Supporting Information

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Supporting Figure 5
Supporting Figure 6
Supporting Figure 7
Supporting Figure 8
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Supporting Figure 5

Fig. 5. Rate of assembly of fragments 1 and 2 (200 mM) over 12 h, monitored at 226 nm after a rapid transition from 90°C to 10°C. The [Q]_max for each sample was calculated as the difference between the ellipticity before denaturation (100% assembled) and the first data point at 10°C, thus omitting the initial jump in ellipticity (which was not resolvable) (1). The value of % assembled was then calculated as the ratio of the observed recovery to [Q]_max. Data were from solutions in 50 mM HOAc(aq) at pH 2.9.

1. Boudko, S., Frank, S., Kammerer, R. A., Stetefeld, J., Schulthess, T., Landwehr, R., Lustig, A., Bächinger, H. P. & Engel, J. (2002) J. Mol. Biol. 317, 459-470.

Supporting Figure 6

Fig. 6. Sedimentation equilibrium data for assemblies of fragments 1 and 2. Data were obtained by analytical ultracentrifugation of fragments (30 mM) in 50 mM potassium phosphate buffer at pH 2.9. (A and C) ln plots of data for (1)_n and (2)_n, respectively, recorded at three speeds at 4°C. (B and D) Species plots of (1)_n and (2)_n data, respectively, derived from analyzing the 12k data as a combination of species from monomer to hexamer.

Supporting Figure 7

Fig. 7. AFM and TEM images of natural type I collagen. (A) AFM height image. (B) Section analysis of data along the direction indicated by the arrow in A. (C) TEM image after rotary shadowing with platinum.

Supporting Figure 8

Fig. 8. AFM images of control samples. (A) Height image of 1 after assembly denaturation (90°C for 15 min). (B) Height image of 2 after assembly denaturation (90°C for 15 min). (C) Height image of 50 mM HOAc(aq) without 1 or 2.