Figure 8 : rfhSP-D adopts a trimer conformation.

From: Efficient protein production inspired by how spiders make silk

Figure 8

(a) Size-exclusion chromatogram of purified rfhSP-D, migrating as a well-defined population of trimeric protein, as confirmed with ESI-MS (Supplementary Fig. 10). (b) SDS-PAGE comparison of rfhSP-D after Ni-sepharose purification (lane 1) and after SEC separation of the main eluting peak (lane 2) shows an unchanged distribution of SDS-stable conformations. The molecular weights in kDa of a protein standard (lane M) are given to the left of the gel figure. (c) The rfhSP-D monomer comprises eight Gly-Xaa-Yaa repeats from the collagenous domain (CD), the α-helical neck domain (ND) and the carbohydrate-recognition domain (CRD). The functional trimer is formed as the neck domains from three monomer units assemble into a coiled-coil motif.