From the Cover: The molecular structure of spider dragline silk: Folding and orientation of the protein backbone -- Data Supplement - Supporting Figure -- Proceedings of the National Academy of Sciences

Supporting information for van Beek et al. (2002) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.152162299

Supporting Figure 6 Fig. 6.
(A) Experimental two-dimensional DOQSY spectra of 1-13C alanine and (B) 1-13C glycine-labeled Nephila edulis silk samples of Fig. 1. C and D show the corresponding best fits when fitting the spectra to a single set of torsion angles (f, y). Line width was a free parameter in the fits, which were performed by using the SIMPLEX and gradient algorithms in minuit [part of the European Center for Nuclear Research (CERN) program library (CERNlib)]. The fits are clearly not satisfactory. The squared deviation, compared to the regulatory approach of Fig. 1, increased by a factor of 4.12 and 3.05 for the alanine- and glycine-labeled samples, respectively.