Characterizing the secondary protein structure of black widow dragline silk using solid-state NMR and X-ray diffraction.

ABSTRACT: This study provides a detailed secondary structural characterization of major ampullate dragline silk from Latrodectus hesperus (black widow) spiders. X-ray diffraction results show that the structure of black widow major ampullate silk fibers is comprised of stacked β-sheet nanocrystallites oriented parallel to the fiber axis and an amorphous region with oriented (anisotropic) and isotropic components. The combination of two-dimensional (2D) (13)C-(13)C through-space and through-bond solid-state NMR experiments provide chemical shifts that are used to determine detailed information about the amino acid motif secondary structure in black widow spider dragline silk. Individual amino acids are incorporated into different repetitive motifs that make up the majority of this protein-based biopo

SUBMITTER: Jenkins JE 

PROVIDER: S-EPMC3914425 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature