Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.

ABSTRACT: Novel site-specific attachment strategies combined with improvements of computational resources enable new insights into the mechanics of the monovalent biotin/streptavidin complex under load and forced us to rethink the diversity of rupture forces reported in the literature. We discovered that the mechanical stability of this complex depends strongly on the geometry in which force is applied. By atomic force microscopy-based single molecule force spectroscopy we found unbinding of biotin to occur beyond 400 pN at force loading rates of 10 nN/s when monovalent streptavidin was tethered at its C-terminus. This value is about twice as high than that for N-terminal attachment. Steered molecular dynamics simulations provided a detailed picture of the mechanics of the unbinding process in the c

SUBMITTER: Sedlak SM 

PROVIDER: S-EPMC6486461 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature