Request a copy

Full Text

• Labeit, D., Watanabe, K., Witt, C., Fujita, H., Wu, Y., Lahmers, S., Funck, T., Labeit, S., Granzier, H., Calcium-dependent molecular spring elements in the giant protein titin. Proc. Natl. Acad. Sci. USA 100 (2003), 13716–13721.
• Javadi, Y., Fernandez, J.M., Perez-Jimenez, R., Protein folding under mechanical forces: a physiological view. Physiology 28 (2013), 9–17.
• Bao, G., Protein mechanics: a new frontier in biomechanics. Exp. Mech. 49 (2009), 153–164.
• Kuhlman, B., Bradley, P., Advances in protein structure prediction and design. Nat. Rev. Mol. Cell Biol. 20 (2019), 681–697.
• Hoffmann, T., Dougan, L., Single molecule force spectroscopy using polyproteins. Chem. Soc. Rev. 41 (2012), 4781–4796.
• Camunas-Soler, J., Ribezzi-Crivellari, M., Ritort, F., Elastic properties of nucleic acids by single-molecule force spectroscopy. Annu. Rev. Biophys. 45 (2016), 65–84.
• Janshoff, A., Neitzert, M., Oberdörfer, Y., Fuchs, H., Force spectroscopy of molecular systems-single moleculespectroscopy of polymers and biomolecules. Angew. Chem. Int. Ed. Engl. 39 (2000), 3212–3237.
• Fisher, T.E., Marszalek, P.E., Fernandez, J.M., Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7 (2000), 719–724.
• Bustamante, C., Chemla, Y.R., Forde, N.R., Izhaky, D., Mechanical processes in biochemistry. Annu. Rev. Biochem. 73 (2004), 705–748.
• Neuman, K.C., Nagy, A., Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat. Methods 5 (2008), 491–505.
• Puchner, E.M., Gaub, H.E., Force and function: probing proteins with AFM-based force spectroscopy. Curr. Opin. Struct. Biol. 19 (2009), 605–614.
• Liang, J., Fernández, J.M., Mechanochemistry: one bond at a time. ACS Nano 3 (2009), 1628–1645.
• Duwez, A.-S., Willet, N., Molecular Manipulation with Atomic Force Microscopy. 2012, CRC Press Press.
• Hughes, M.L., Dougan, L., The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding. Rep. Prog. Phys., 79, 2016, 076601.
• Giannotti, M.I., Vancso, G.J., Interrogation of single synthetic polymer chains and polysaccharides by AFM-based force spectroscopy. ChemPhysChem 8 (2007), 2290–2307.
• Oesterhelt, F., Rief, M., Gaub, H.E., Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water. New J. Phys., 1, 1999, 6.
• Marszalek, P.E., Oberhauser, A.F., Pang, Y.P., Fernandez, J.M., Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring. Nature 396 (1998), 661–664.
• Rief, M., Oesterhelt, F., Heymann, B., Gaub, H.E., Single molecule force spectroscopy on polysaccharides by atomic force microscopy. Science 275 (1997), 1295–1297.
• Guichard, G., Huc, I., Synthetic foldamers. Chem. Commun. 47 (2011), 5933–5941.
• Cheng, R.P., Gellman, S.H., DeGrado, W.F., β-peptides: From structure to function. Chem. Rev. 101 (2001), 3219–3232.
• Yashima, E., Maeda, K., Iida, H., Furusho, Y., Nagai, K., Helical polymers: synthesis, structures, and functions. Chem. Rev. 109 (2009), 6102–6211.
• Yashima, E., Ousaka, N., Taura, D., Shimomura, K., Ikai, T., Maeda, K., Supramolecular helical systems: helical assemblies of small molecules, foldamers, and polymers with chiral amplification and their functions. Chem. Rev. 116 (2016), 13752–13990.
• Kim, J.S., Jung, Y.J., Park, J.W., Shaller, A.D., Wan, W., Li, A.D.Q., Mechanically stretching folded nano- π-b; -stacks reveals pico-newton attractive forces. Adv. Mater. 21 (2009), 786–789.
• Sluysmans, D., Zhang, L., Li, X., Garci, A., Stoddart, J.F., Duwez, A.S., Viologen tweezers to probe the force of individual donor−acceptor π-interactions. J. Am. Chem. Soc. 142 (2020), 21153–21159.
• Sluysmans, D., Willet, N., Thevenot, J., Lecommandoux, S., Duwez, A.S., Single- molecule mechanical unfolding experiments reveal a critical length for the formation of α-helices in peptides. Nanoscale Horiz 5 (2020), 671–678.
• Lussis, P., Svaldo-Lanero, T., Bertocco, A., Fustin, C.A., Leigh, D.A., Duwez, A.S., A single synthetic small molecule that generates force against a load. Nat. Nanotechnol. 6 (2011), 553–557.
• Van Quaethem, A., Lussis, P., Leigh, D.A., Duwez, A.-S., Fustin, C.-A., Probing the mobility of catenane rings in single molecules. Chem. Sci. 5 (2014), 1449–1452.
• Sluysmans, D., Hubert, S., Bruns, C.J., Zhu, Z., Stoddart, J.F., Duwez, A.S., Synthetic oligorotaxanes exert high forces when folding under mechanical load. Nat. Nanotechnol. 13 (2018), 209–213.
• Sluysmans, D., Devaux, F., Bruns, C.J., Stoddart, J.F., Duwez, A.S., Dynamic force spectroscopy of synthetic oligorotaxane foldamers. Proc. Natl. Acad. Sci. USA 115 (2018), 9362–9366.
• Huc, I., Aromatic oligoamide foldamers. Eur. J. Org. Chem. 2004 (2004), 17–29.
• Zhang, D.W., Zhao, X., Hou, J.L., Li, Z.T., Aromatic amide foldamers: structures, properties, and functions. Chem. Rev. 112 (2012), 5271–5316.
• Qi, T., Deschrijver, T., Huc, I., Large-scale and chromatography-free synthesis of an octameric quinoline-based aromatic amide helical foldamer. Nat. Protoc. 8 (2013), 693–708.
• Jiang, H., Léger, J.M., Huc, I., Aromatic δ-peptides. J. Am. Chem. Soc. 125 (2003), 3448–3449.
• Nelson, J.C., Saven, J.G., Moore, J.S., Wolynes, P.G., Solvophobically driven folding of nonbiological oligomers. Science 277 (1997), 1793–1796.
• Gong, B., Zeng, H., Zhu, J., Yuan, L., Han, Y., Cheng, S., Furukawa, M., Parra, R.D., Kovalevsky, A.Y., Mills, J.L., et al. Creating nanocavities of tunable sizes: hollow helices. Proc. Natl. Acad. Sci. USA 99 (2002), 11583–11588.
• Ohkita, M., Lehn, J.M., Baum, G., Fenske, D., Helicity coding: programmed molecular self-organization of achiral nonbiological strands into multiturn helical superstructures: synthesis and characterization of alternating pyridine-pyrimidine oligomers. Chem. Eur. J. 5 (1999), 3471–3481.
• Qi, T., Maurizot, V., Noguchi, H., Charoenraks, T., Kauffmann, B., Takafuji, M., Ihara, H., Huc, I., Solvent dependence of helix stability in aromatic oligoamide foldamers. Chem. Commun., 48, 2012, 6337.
• Delsuc, N., Kawanami, T., Lefeuvre, J., Shundo, A., Ihara, H., Takafuji, M., Huc, I., Kinetics of helix-handedness inversion: folding and unfolding in aromatic amide oligomers. ChemPhysChem 9 (2008), 1882–1890.
• Abramyan, A.M., Liu, Z., Pophristic, V., Helix handedness inversion in arylamide foldamers: elucidation and free energy profile of a hopping mechanism. Chem. Commun. 52 (2016), 669–672.
• Li, X., Qi, T., Srinivas, K., Massip, S., Maurizot, V., Huc, I., Synthesis and multibromination of nanosized helical aromatic amide foldamers via segment-doubling condensation. Org. Lett. 18 (2016), 1044–1047.
• Ziach, K., Chollet, C., Parissi, V., Prabhakaran, P., Marchivie, M., Corvaglia, V., Bose, P.P., Laxmi-Reddy, K., Godde, F., Schmitter, J.-M., et al. Single helically folded aromatic oligoamides that mimic the charge surface of double-stranded B-DNA. Nat. Chem. 10 (2018), 511–518.
• Chandramouli, N., Ferrand, Y., Lautrette, G., Kauffmann, B., MacKereth, C.D., Laguerre, M., Dubreuil, D., Huc, I., Iterative design of a helically folded aromatic oligoamide sequence for the selective encapsulation of fructose. Nat. Chem. 7 (2015), 334–341.
• Méndez-Ardoy, A., Markandeya, N., Li, X., Tsai, Y.T., Pecastaings, G., Buffeteau, T., Maurizot, V., Muccioli, L., Castet, F., Huc, I., Bassani, D.M., Multi-dimensional charge transport in supramolecular helical foldamer assemblies. Chem. Sci. 8 (2017), 7251–7257.
• Li, X., Markandeya, N., Jonusauskas, G., McClenaghan, N.D., Maurizot, V., Denisov, S.A., Huc, I., Photoinduced electron transfer and hole migration in nanosized helical aromatic oligoamide foldamers. J. Am. Chem. Soc. 138 (2016), 13568–13578.
• Rief, M., Pascual, J., Saraste, M., Gaub, H.E., Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286 (1999), 553–561.
• Berkemeier, F., Bertz, M., Xiao, S., Pinotsis, N., Wilmanns, M., Gräter, F., Rief, M., Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin. Proc. Natl. Acad. Sci. USA 108 (2011), 14139–14144.
• Schwaiger, I., Sattler, C., Hostetter, D.R., Rief, M., The myosin coiled-coil is a truly elastic protein structure. Nat. Mater. 1 (2002), 232–235.
• Li, L., Wetzel, S., Plückthun, A., Fernandez, J.M., Stepwise unfolding of ankyrin repeats in a single protein revealed by atomic force microscopy. Biophys. J. 90 (2006), L30–L32.
• Takahashi, H., Rico, F., Chipot, C., Scheuring, S., α-helix unwinding as force buffer in spectrins. ACS Nano 12 (2018), 2719–2727.
• Cluzel, P., Lebrun, A., Heller, C., Lavery, R., Viovy, J.L., Chatenay, D., Caron, F., DNA: an extensible molecule. Science 271 (1996), 792–794.
• Smith, S.B., Cui, Y., Bustamante, C., Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271 (1996), 795–799.
• Zhang, Q., Marszalek, P.E., Identification of sugar isomers by single-molecule force spectroscopy. J. Am. Chem. Soc. 128 (2006), 5596–5597.
• Zhang, L., Wang, C., Cui, S., Wang, Z., Zhang, X., Single-molecule force spectroscopy on curdlan: unwinding helical structures and random coils. Nano Lett 3 (2003), 1119–1124.
• Zegarra, F.C., Peralta, G.N., Coronado, A.M., Gao, Y.Q., Free energies and forces in helix–coil transition of homopolypeptides under stretching. Phys. Chem. Chem. Phys. 11 (2009), 4019–4024.
• Zoldák, G., Stigler, J., Pelz, B., Li, H., Rief, M., Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy. Proc. Natl. Acad. Sci. USA 110 (2013), 18156–18161.
• Rico, F., Gonzalez, L., Casuso, I., Puig-Vidal, M., Scheuring, S., High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations. Science 342 (2013), 741–743.
• Yu, H., Siewny, M.G.W., Edwards, D.T., Sanders, A.W., Perkins, T.T., Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins. Science 355 (2017), 945–950.
• Puchner, E.M., Franzen, G., Gautel, M., Gaub, H.E., Comparing proteins by their unfolding pattern. Biophys. J. 95 (2008), 426–434.
• Uribe, L., Gauss, J., Diezemann, G., Determining factors for the unfolding pathway of peptides, peptoids, and peptidic foldamers. J. Phys. Chem. B 120 (2016), 10433–10441.
• Parent, L.R., Bakalis, E., Ramírez-Hernández, A., Kammeyer, J.K., Park, C., de Pablo, J., Zerbetto, F., Patterson, J.P., Gianneschi, N.C., Directly observing micelle fusion and growth in solution by liquid-cell transmission electron microscopy. J. Am. Chem. Soc. 139 (2017), 17140–17151.
• Parent, L.R., Bakalis, E., Proetto, M., Li, Y., Park, C., Zerbetto, F., Gianneschi, N.C., Tackling the challenges of dynamic experiments using liquid-cell transmission electron microscopy. Acc. Chem. Res. 51 (2018), 3–11.
• Bakalis, E., Parent, L.R., Vratsanos, M., Park, C., Gianneschi, N.C., Zerbetto, F., Complex nanoparticle diffusional motion in liquid-cell transmission electron microscopy. J. Phys. Chem. C 124 (2020), 14881–14890.
• Zwanzig, R., Szabo, A., Bagchi, B., Levinthal's paradox. Proc. Natl. Acad. Sci. USA 89 (1992), 20–22.
• Karplus, M., The Levinthal paradox: yesterday and today. Fold. Des. 2 (1997), S69–S75.