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.
Item Type: | Journal article |
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Faculties: | Physics |
Subjects: | 500 Science > 530 Physics |
ISSN: | 2470-0045 |
Language: | English |
Item ID: | 47631 |
Date Deposited: | 27. Apr 2018, 08:13 |
Last Modified: | 07. May 2024, 18:15 |