Streptavidin/biotin: Tethering geometry defines unbinding mechanics-Reference-Cited by-同舟云学术

Streptavidin/biotin: Tethering geometry defines unbinding mechanics

Published:2020-03-27 Issue:13 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Sedlak Steffen M.¹^ORCID,Schendel Leonard C.¹^ORCID,Gaub Hermann E.¹^ORCID,Bernardi Rafael C.²^ORCID

Affiliation:

1. Lehrstuhl für Angewandte Physik and Center for NanoScience, Ludwig-Maximilians-Universität München, Amalienstr. 54, 80799 Munich, Germany.

2. NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Abstract

Single-molecule force spectroscopy reveals how the mechanical stability of a widely used biomolecular complex varies fourfold.

Funder

National Science Foundation

National Institutes of Health

Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference48 articles.

1. Molecular mechanism of extreme mechanostability in a pathogen adhesin

2. Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A

3. Pulling Direction as a Reaction Coordinate for the Mechanical Unfolding of Single Molecules

4. Intermolecular Forces and Energies Between Ligands and Receptors

5. Sensing Discrete Streptavidin-Biotin Interactions with Atomic Force Microscopy

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