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      Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly

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          Abstract

          Multi-step assembly of individual protein building blocks is key to the formation of essential higher-order structures inside and outside of cells. Optical tweezers is a technique well suited to investigate the mechanics and dynamics of these structures at a variety of size scales. In this mini-review, we highlight experiments that have used optical tweezers to investigate protein assembly and mechanics, with a focus on the extracellular matrix protein collagen. These examples demonstrate how optical tweezers can be used to study mechanics across length scales, ranging from the single-molecule level to fibrils to protein networks. We discuss challenges in experimental design and interpretation, opportunities for integration with other experimental modalities, and applications of optical tweezers to current questions in protein mechanics and assembly.

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          Most cited references122

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          The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

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            Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy.

            Single-molecule force spectroscopy has emerged as a powerful tool to investigate the forces and motions associated with biological molecules and enzymatic activity. The most common force spectroscopy techniques are optical tweezers, magnetic tweezers and atomic force microscopy. Here we describe these techniques and illustrate them with examples highlighting current capabilities and limitations.
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              Microtubules acquire resistance from mechanical breakage through intralumenal acetylation.

              Eukaryotic cells rely on long-lived microtubules for intracellular transport and as compression-bearing elements. We considered that long-lived microtubules are acetylated inside their lumen and that microtubule acetylation may modify microtubule mechanics. Here, we found that tubulin acetylation is required for the mechanical stabilization of long-lived microtubules in cells. Depletion of the tubulin acetyltransferase TAT1 led to a significant increase in the frequency of microtubule breakage. Nocodazole-resistant microtubules lost upon removal of acetylation were largely restored by either pharmacological or physical removal of compressive forces. In in vitro reconstitution experiments, acetylation was sufficient to protect microtubules from mechanical breakage. Thus, acetylation increases mechanical resilience to ensure the persistence of long-lived microtubules.
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                Author and article information

                Contributors
                Journal
                Front Mol Biosci
                Front Mol Biosci
                Front. Mol. Biosci.
                Frontiers in Molecular Biosciences
                Frontiers Media S.A.
                2296-889X
                06 October 2020
                2020
                : 7
                : 577314
                Affiliations
                [1] 1Department of Physics, Simon Fraser University , Burnaby, BC, Canada
                [2] 2Soft Condensed Matter and Biophysics, Utrecht University , Utrecht, Netherlands
                [3] 3School of Engineering and Applied Sciences, Harvard University , Cambridge, MA, United States
                [4] 4Department of Molecular Biology and Biochemistry, Simon Fraser University , Burnaby, BC, Canada
                [5] 5Department of Chemistry, Simon Fraser University , Burnaby, BC, Canada
                [6] 6Centre for Cell Biology, Development and Disease (C2D2), Simon Fraser University , Burnaby, BC, Canada
                Author notes

                Edited by: Daryl Preece, University of California, San Diego, United States

                Reviewed by: Ron Orbach, Yale University, United States; Seok-Cheol Hong, Korea University, South Korea

                *Correspondence: Nancy R. Forde, nforde@ 123456sfu.ca

                This article was submitted to Nanobiotechnology, a section of the journal Frontiers in Molecular Biosciences

                Article
                10.3389/fmolb.2020.577314
                7573139
                33134316
                89eb903c-1fe7-40b8-85a9-00322f069728
                Copyright © 2020 Lehmann, Shayegan, Blab and Forde.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 29 June 2020
                : 27 August 2020
                Page count
                Figures: 2, Tables: 0, Equations: 0, References: 126, Pages: 10, Words: 0
                Funding
                Funded by: Natural Sciences and Engineering Research Council of Canada 10.13039/501100000038
                Funded by: Deutsche Forschungsgemeinschaft 10.13039/501100001659
                Funded by: Fonds Québécois de la Recherche sur la Nature et les Technologies 10.13039/501100003150
                Categories
                Molecular Biosciences
                Mini Review

                optical tweezers (ot),protein mechanics,single molecule,microrheology,collagen,protein structure/folding,protein assemblies,fibrillar proteins

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