Open AccessStreptavidin/biotin: Tethering geometry defines unbinding mechanics
Author(s) -
Steffen M. Sedlak,
Leonard C. Schendel,
Hermann E. Gaub,
Rafael C. Bernardi
Publication year - 2020
Publication title -
science advances
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 5.928
H-Index - 146
ISSN - 2375-2548
DOI - 10.1126/sciadv.aay5999
Subject(s) - force spectroscopy , tethering , streptavidin , biotin , molecular dynamics , umbrella sampling , chemical physics , chemistry , molecule , macromolecule , biophysics , nanotechnology , avidin , nanobiotechnology , atomic force microscopy , materials science , computational chemistry , biochemistry , biology , microbiology and biotechnology , organic chemistry , nanoparticle
Single-molecule force spectroscopy reveals how the mechanical stability of a widely used biomolecular complex varies fourfold.
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