Biasing effects of receptor-ligand complexes on protein-unfolding statistics

Constantin Schoeler, Tobias Verdorfer, Hermann E. Gaub, and Michael A. Nash
Phys. Rev. E 94, 042412 – Published 13 October 2016

Abstract

Protein receptor-ligand pairs are increasingly used as specific molecular handles in single-molecule protein-unfolding experiments. Further, known marker domains, also referred to as fingerprints, provide unique unfolding signatures to identify specific single-molecule interactions, when receptor-ligand pairs themselves are investigated. We show here that in cases where there is an overlap between the probability distribution associated with fingerprint domain unfolding and that associated with receptor-ligand dissociation, the experimentally measured force distributions are mutually biased. This biasing effect masks the true parameters of the underlying free energy landscape. To address this, we present a model-free theoretical framework that corrects for the biasing effect caused by such overlapping distributions.

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  • Received 30 May 2016

DOI:https://doi.org/10.1103/PhysRevE.94.042412

©2016 American Physical Society

Physics Subject Headings (PhySH)

Physics of Living Systems

Authors & Affiliations

Constantin Schoeler1, Tobias Verdorfer1, Hermann E. Gaub1, and Michael A. Nash1,2,3,*

  • 1Lehrstuhl für Angewandte Physik and Center for Nanoscience, Ludwig-Maximilians-Universität München, Amalienstr. 54, 80799 Munich, Germany
  • 2Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel, Switzerland
  • 3Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule Zürich (ETH-Zürich), 4058 Basel, Switzerland

  • *michael.nash@unibas.ch

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Issue

Vol. 94, Iss. 4 — October 2016

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