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Journal articles on the topic 'Biomolecular motors'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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1

Hess, Henry, and George D. Bachand. "Biomolecular motors." Materials Today 8, no. 12 (December 2005): 22–29. http://dx.doi.org/10.1016/s1369-7021(05)71286-4.

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2

Hess, Henry, and Jung-Chi Liao. "Special Issue: Biomolecular Motors and Motor Assemblies." Cellular and Molecular Bioengineering 6, no. 1 (January 3, 2013): 1–2. http://dx.doi.org/10.1007/s12195-012-0268-1.

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3

Hess, Henry, and Gadiel Saper. "Engineering with Biomolecular Motors." Accounts of Chemical Research 51, no. 12 (October 30, 2018): 3015–22. http://dx.doi.org/10.1021/acs.accounts.8b00296.

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4

KAKUGO, Akira. "Integration of Biomolecular Motors." KOBUNSHI RONBUNSHU 65, no. 8 (2008): 506–15. http://dx.doi.org/10.1295/koron.65.506.

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5

Hess, Henry, George D. Bachand, and Viola Vogel. "Powering Nanodevices with Biomolecular Motors." Chemistry - A European Journal 10, no. 9 (May 3, 2004): 2110–16. http://dx.doi.org/10.1002/chem.200305712.

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6

Hess, Henry. "Engineering Applications of Biomolecular Motors." Annual Review of Biomedical Engineering 13, no. 1 (August 15, 2011): 429–50. http://dx.doi.org/10.1146/annurev-bioeng-071910-124644.

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7

Karplus, Martin, and Yi Qin Gao. "Biomolecular motors: the F1-ATPase paradigm." Current Opinion in Structural Biology 14, no. 2 (April 2004): 250–59. http://dx.doi.org/10.1016/j.sbi.2004.03.012.

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8

NOJI, Hiroyuki. "Biomolecular Motors as Nanometer-sized Actuators." Journal of the Society of Mechanical Engineers 108, no. 1042 (2005): 738–39. http://dx.doi.org/10.1299/jsmemag.108.1042_738.

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9

Wagoner, Jason A., and Ken A. Dill. "Evolution of mechanical cooperativity among myosin II motors." Proceedings of the National Academy of Sciences 118, no. 20 (May 11, 2021): e2101871118. http://dx.doi.org/10.1073/pnas.2101871118.

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Myosin II is a biomolecular machine that is responsible for muscle contraction. Myosin II motors act cooperatively: during muscle contraction, multiple motors bind to a single actin filament and pull it against an external load, like people pulling on a rope in a tug-of-war. We model the dynamics of actomyosin filaments in order to study the evolution of motor–motor cooperativity. We find that filament backsliding—the distance an actin slides backward when a motor at the end of its cycle releases—is central to the speed and efficiency of muscle contraction. Our model predicts that this backsliding has been reduced through evolutionary adaptations to the motor’s binding propensity, the strength of the motor’s power stroke, and the force dependence of the motor’s release from actin. These properties optimize the collective action of myosin II motors, which is not a simple sum of individual motor actions. The model also shows that these evolutionary variables can explain the speed–efficiency trade-off observed across different muscle tissues. This is an example of how evolution can tune the microscopic properties of individual proteins in order to optimize complex biological functions.
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10

Montemagno, Carlo, and George Bachand. "Constructing nanomechanical devices powered by biomolecular motors." Nanotechnology 10, no. 3 (August 12, 1999): 225–31. http://dx.doi.org/10.1088/0957-4484/10/3/301.

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11

Bachand, George D., Henry Hess, Banahalli Ratna, Peter Satir, and Viola Vogel. "“Smart dust” biosensors powered by biomolecular motors." Lab on a Chip 9, no. 12 (2009): 1661. http://dx.doi.org/10.1039/b821055a.

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12

Yokokawa, R., S. Takeuchi, T. Kon, M. Nishiura, R. Ohkura, M. Edamatsu, K. Sutoh, and H. Fujita. "Hybrid Nanotransport System by Biomolecular Linear Motors." Journal of Microelectromechanical Systems 13, no. 4 (August 2004): 612–19. http://dx.doi.org/10.1109/jmems.2004.832193.

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13

McLaughlin, R. Tyler, Michael R. Diehl, and Anatoly B. Kolomeisky. "Collective dynamics of processive cytoskeletal motors." Soft Matter 12, no. 1 (2016): 14–21. http://dx.doi.org/10.1039/c5sm01609f.

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14

Kabir, Arif Md Rashedul, and Akira Kakugo. "Study of active self-assembly using biomolecular motors." Polymer Journal 50, no. 12 (September 7, 2018): 1139–48. http://dx.doi.org/10.1038/s41428-018-0109-8.

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15

Bachand, George D., Nathan F. Bouxsein, Virginia VanDelinder, and Marlene Bachand. "Biomolecular motors in nanoscale materials, devices, and systems." Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology 6, no. 2 (December 11, 2013): 163–77. http://dx.doi.org/10.1002/wnan.1252.

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16

Yokokawa, R., S. Takeuchi, T. Kon, M. Nishiura, K. Sutoh, and H. Fujita. "Control of Biomolecular Motors for Nano Transfer System." Proceedings of JSME annual Conference on Robotics and Mechatronics (Robomec) 2003 (2003): 116. http://dx.doi.org/10.1299/jsmermd.2003.116_3.

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17

Katira, Parag, Isaac Luria, Shruti Seshadri, and Henry Hess. "Self-assembly via Active Transport By Biomolecular Motors." Biophysical Journal 96, no. 3 (February 2009): 6a. http://dx.doi.org/10.1016/j.bpj.2008.12.924.

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18

Grant, Barry J. "Biomolecular Motors and Switches: From Machines to Drugs." Biophysical Journal 102, no. 3 (January 2012): 698a. http://dx.doi.org/10.1016/j.bpj.2011.11.3792.

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19

Kiani, Farooq Ahmad, and Stefan Fischer. "Comparing the catalytic strategy of ATP hydrolysis in biomolecular motors." Physical Chemistry Chemical Physics 18, no. 30 (2016): 20219–33. http://dx.doi.org/10.1039/c6cp01364c.

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20

Yoshida, Y., S. Takeuchi, and T. Nishizaka. "1P176 Micro-patterning of biomolecular motors by MEMS technology." Seibutsu Butsuri 45, supplement (2005): S75. http://dx.doi.org/10.2142/biophys.45.s75_4.

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21

YAGI, Ichiro, and Takahiro NITTA. "Translation Mechanism of Molecular Shuttles Driven by Biomolecular Motors." Proceedings of JSME annual Conference on Robotics and Mechatronics (Robomec) 2017 (2017): 2P2—P01. http://dx.doi.org/10.1299/jsmermd.2017.2p2-p01.

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22

Peterman, Erwin J. G., Hernando Sosa, and W. E. Moerner. "SINGLE-MOLECULE FLUORESCENCE SPECTROSCOPY AND MICROSCOPY OF BIOMOLECULAR MOTORS." Annual Review of Physical Chemistry 55, no. 1 (June 2004): 79–96. http://dx.doi.org/10.1146/annurev.physchem.55.091602.094340.

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23

Hess, H. "MATERIALS SCIENCE: Enhanced: Toward Devices Powered by Biomolecular Motors." Science 312, no. 5775 (May 12, 2006): 860–61. http://dx.doi.org/10.1126/science.1126399.

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24

Liu, Ming S., B. D. Todd, and Richard J. Sadus. "A mechanochemical theory for the ATP-fuelled biomolecular motors." International Journal of Nanotechnology 6, no. 12 (2009): 1121. http://dx.doi.org/10.1504/ijnt.2009.028468.

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25

Trigueros, Sonia, Sonia Contera, and John Ryan. "DNA Conformation and Biomolecular Motors: New Nanomedicine Research Targets." Biophysical Journal 96, no. 3 (February 2009): 345a. http://dx.doi.org/10.1016/j.bpj.2008.12.1734.

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26

Shah, Zameer Hussain, Shuo Wang, Longbin Xian, Xuemao Zhou, Yi Chen, Guanhua Lin, and Yongxiang Gao. "Highly efficient chemically-driven micromotors with controlled snowman-like morphology." Chemical Communications 56, no. 97 (2020): 15301–4. http://dx.doi.org/10.1039/d0cc06812h.

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27

Feizabadi, Mitra Shojania, Ramiz S. Alejilat, Alexis B. Duffy, Jane C. Breslin, and Ibukunoluwa I. Akintola. "A Confirmation for the Positive Electric Charge of Bio-Molecular Motors through Utilizing a Novel Nano-Technology Approach In Vitro." International Journal of Molecular Sciences 21, no. 14 (July 13, 2020): 4935. http://dx.doi.org/10.3390/ijms21144935.

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Molecular motors are microtubule-based proteins which contribute to many cell functions, such as intracellular transportation and cell division. The details of the nature of the mutual interactions between motors and microtubules still needs to be extensively explored. However, electrostatic interaction is known as one of the key factors making motor-microtubule association possible. The association rate of molecular motors to microtubules is a way to observe and evaluate the charge of the bio-motors in vivo. Growing evidence indicates that microtubules with distinct structural compositions in terms of beta tubulin isotypes carry different charges. Therefore, the electrostatic-driven association rate of motors–microtubules, which is a base for identifying the charge of motors, can be more likely influenced. Here, we present a novel method to experimentally confirm the charge of molecular motors in vitro. The offered nanotechnology-based approach can validate the charge of motors in the absence of any cellular components through the observation and analysis of the changes that biomolecular motors can cause on the dynamic of charged microspheres inside a uniform electric field produced by a microscope slide-based nanocapacitor. This new in vitro experimental method is significant as it minimizes the intracellular factors that may interfere the electric charge that molecular motors carry.
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28

Agarwal, Ashutosh, and Henry Hess. "Biomolecular motors at the intersection of nanotechnology and polymer science." Progress in Polymer Science 35, no. 1-2 (January 2010): 252–77. http://dx.doi.org/10.1016/j.progpolymsci.2009.10.007.

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29

NITTA, Takahiro, and Yuki ISHIGURE. "1P1-P10 Simulation of material transport systems by biomolecular motors." Proceedings of JSME annual Conference on Robotics and Mechatronics (Robomec) 2015 (2015): _1P1—P10_1—_1P1—P10_2. http://dx.doi.org/10.1299/jsmermd.2015._1p1-p10_1.

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30

Jamali, Y., A. Lohrasebi, and H. Rafii-Tabar. "Computational modelling of the stochastic dynamics of kinesin biomolecular motors." Physica A: Statistical Mechanics and its Applications 381 (July 2007): 239–54. http://dx.doi.org/10.1016/j.physa.2007.03.022.

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31

Lin, Chih-Ting, Ming-Tse Kao, Katsuo Kurabayashi, and Edgar Meyhöfer. "Efficient Designs for Powering Microscale Devices with Nanoscale Biomolecular Motors." Small 2, no. 2 (February 2006): 281–87. http://dx.doi.org/10.1002/smll.200500153.

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32

Furuta, Akane, Misako Amino, Maki Yoshio, Kazuhiro Oiwa, Hiroaki Kojima, and Ken'ya Furuta. "Creating biomolecular motors based on dynein and actin-binding proteins." Nature Nanotechnology 12, no. 3 (November 14, 2016): 233–37. http://dx.doi.org/10.1038/nnano.2016.238.

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33

Kakugo, Akira, Kazuhiro Shikinaka, Ryuzo Kawamura, and JianPing Gong. "Integration of biomolecular motors — Toward an ATP fueled soft biomachine." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 151, no. 4 (December 2008): 444. http://dx.doi.org/10.1016/j.cbpb.2008.09.062.

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34

Yoshida, Yumi, Ryuji Yokokawa, Hiroaki Suzuki, Kyoko Atsuta, Hiroyuki Fujita, and Shoji Takeuchi. "Biomolecular linear motors confined to move upon micro-patterns on glass." Journal of Micromechanics and Microengineering 16, no. 8 (June 26, 2006): 1550–54. http://dx.doi.org/10.1088/0960-1317/16/8/015.

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35

Bachand, G. D., R. K. Soong, H. P. Neves, A. Olkhovets, H. G. Craighead, and C. D. Montemagno. "Precision Attachment of Individual F1-ATPase Biomolecular Motors on Nanofabricated Substrates." Nano Letters 1, no. 1 (January 2001): 42–44. http://dx.doi.org/10.1021/nl005513i.

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36

Wagoner, Jason A., and Ken A. Dill. "Opposing Pressures of Speed and Efficiency Guide the Evolution of Molecular Machines." Molecular Biology and Evolution 36, no. 12 (August 20, 2019): 2813–22. http://dx.doi.org/10.1093/molbev/msz190.

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Abstract Many biomolecular machines need to be both fast and efficient. How has evolution optimized these machines along the tradeoff between speed and efficiency? We explore this question using optimizable dynamical models along coordinates that are plausible evolutionary degrees of freedom. Data on 11 motors and ion pumps are consistent with the hypothesis that evolution seeks an optimal balance of speed and efficiency, where any further small increase in one of these quantities would come at great expense to the other. For FoF1-ATPases in different species, we also find apparent optimization of the number of subunits in the c-ring, which determines the number of protons pumped per ATP synthesized. Interestingly, these ATPases appear to more optimized for efficiency than for speed, which can be rationalized through their key role as energy transducers in biology. The present modeling shows how the dynamical performance properties of biomolecular motors and pumps may have evolved to suit their corresponding biological actions.
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37

Xie, Ping. "Non-tight and tight chemomechanical couplings of biomolecular motors under hindering loads." Journal of Theoretical Biology 490 (April 2020): 110173. http://dx.doi.org/10.1016/j.jtbi.2020.110173.

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38

Magdum, Sandip S. "Functions and Future Applications of F1 ATPase as Nanobioengine - Powering the Nanoworld!" Nano Hybrids 5 (October 2013): 33–53. http://dx.doi.org/10.4028/www.scientific.net/nh.5.33.

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Recent nanotechnological revolution mandates astonishing imagination about future nanoworld. Nature has ability to create nanobiomolecules which can function in extraordinary way which can be used to produce nanohybrid systems. The opportunity to use such nanobiomolecules in combination of nanomechanical systems for development of novel nanohybrid systems for their various applications needs to explore in further nanotechnological development. F1 ATPase is a subunit of ATP synthase, which is one of the biomolecular structure works on the plasma membrane of the living cell. The reversible function of F1 ATPase gives a counterclockwise rotation of γ shaft by hydrolyzing ATP and the energy released in the form of rotational torque. This rotational torque of F1 ATPase can be used to power the functional movement of nanodevice. This feature article discusses comparisons of various biomolecular motors for their powering capacities, recent developments, presents new discoveries, experimentations on F1 ATPase and its novel imaginary futuristic applications where F1 ATPase could be used as nanobioengine for powering functional nanoworld.
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39

Okazaki, Kei-ichi, Akihiko Nakamura, and Ryota Iino. "Chemical-State-Dependent Free Energy Profile from Single-Molecule Trajectories of Biomolecular Motors: Application to Processive Chitinase." Journal of Physical Chemistry B 124, no. 30 (July 6, 2020): 6475–87. http://dx.doi.org/10.1021/acs.jpcb.0c02698.

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40

Okazaki, Kei-ichi, Akihiko Nakamura, and Ryota Iino. "Chemical-State-Dependent Free Energy Profile from Single-Molecule Trajectories of Biomolecular Motors: Application to Processive Chitinase." Biophysical Journal 120, no. 3 (February 2021): 270a. http://dx.doi.org/10.1016/j.bpj.2020.11.1721.

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41

Lohrasebi, A., Y. Jamali, and H. Rafii-Tabar. "Modeling the effect of external electric field and current on the stochastic dynamics of ATPase nano-biomolecular motors." Physica A: Statistical Mechanics and its Applications 387, no. 22 (September 2008): 5466–76. http://dx.doi.org/10.1016/j.physa.2008.05.030.

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42

Wasylycia, Joshua R., Svetlana Sapelnikova, Hyuk Jeong, Jelena Dragoljic, Sandra L. Marcus, and D. Jed Harrison. "Nano-biopower supplies for biomolecular motors: the use of metabolic pathway-based fuel generating systems in microfluidic devices." Lab on a Chip 8, no. 6 (2008): 979. http://dx.doi.org/10.1039/b801033a.

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43

Qiang, Cui. "3SBA-03 Molecular simulations of proton pumps and biomolecular motors(Rise of molecular machines,Symposium,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))." Seibutsu Butsuri 54, supplement1-2 (2014): S137. http://dx.doi.org/10.2142/biophys.54.s137_1.

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44

Lohrasebi, A., S. Mohamadi, S. Fadaie, and H. Rafii-Tabar. "Modelling the influence of thermal effects induced by radio frequency electric field on the dynamics of the ATPase nano-biomolecular motors." Physica Medica 28, no. 3 (July 2012): 221–29. http://dx.doi.org/10.1016/j.ejmp.2011.07.004.

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45

Hassan, Hammad Ali, Sadaf Rani, Tabeer Fatima, Farooq Ahmad Kiani, and Stefan Fischer. "Effect of protonation on the mechanism of phosphate monoester hydrolysis and comparison with the hydrolysis of nucleoside triphosphate in biomolecular motors." Biophysical Chemistry 230 (November 2017): 27–35. http://dx.doi.org/10.1016/j.bpc.2017.08.003.

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46

Seifert, Udo. "From Stochastic Thermodynamics to Thermodynamic Inference." Annual Review of Condensed Matter Physics 10, no. 1 (March 10, 2019): 171–92. http://dx.doi.org/10.1146/annurev-conmatphys-031218-013554.

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For a large class of nonequilibrium systems, thermodynamic notions like work, heat, and, in particular, entropy production can be identified on the level of fluctuating dynamical trajectories. Within stochastic thermodynamics various fluctuation theorems relating these quantities have been proven. Their application to experimental systems requires that all relevant mesostates are accessible. Recent advances address the typical situation that only partial, or coarse-grained, information about a system is available. Thermodynamic inference as a general strategy uses consistency constraints derived from stochastic thermodynamics to infer otherwise hidden properties of nonequilibrium systems. An important class in this respect are active particles, for which we resolve the conflicting strategies that have been proposed to identify entropy production. As a paradigm for thermodynamic inference, the thermodynamic uncertainty relation provides a lower bound on the entropy production through measurements of the dispersion of any current in the system. Likewise, it quantifies the cost of precision for biomolecular processes. Generalizations and ramifications allow the inference of, inter alia, model-free upper bounds on the efficiency of molecular motors and of the minimal number of intermediate states in enzymatic networks.
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47

Volkán-Kacsó, Sándor, and Rudolph A. Marcus. "Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPase." Proceedings of the National Academy of Sciences 113, no. 43 (October 10, 2016): 12029–34. http://dx.doi.org/10.1073/pnas.1611601113.

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A recently proposed chemomechanical group transfer theory of rotary biomolecular motors is applied to treat single-molecule controlled rotation experiments. In these experiments, single-molecule fluorescence is used to measure the binding and release rate constants of nucleotides by monitoring the occupancy of binding sites. It is shown how missed events of nucleotide binding and release in these experiments can be corrected using theory, with F1-ATP synthase as an example. The missed events are significant when the reverse rate is very fast. Using the theory the actual rate constants in the controlled rotation experiments and the corrections are predicted from independent data, including other single-molecule rotation and ensemble biochemical experiments. The effective torsional elastic constant is found to depend on the binding/releasing nucleotide, and it is smaller for ADP than for ATP. There is a good agreement, with no adjustable parameters, between the theoretical and experimental results of controlled rotation experiments and stalling experiments, for the range of angles where the data overlap. This agreement is perhaps all the more surprising because it occurs even though the binding and release of fluorescent nucleotides is monitored at single-site occupancy concentrations, whereas the stalling and free rotation experiments have multiple-site occupancy.
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48

Kim, Taesung, Li-Jing Cheng, Ming-Tse Kao, Ernest F. Hasselbrink, LingJie Guo, and Edgar Meyhöfer. "Biomolecular motor-driven molecular sorter." Lab on a Chip 9, no. 9 (2009): 1282. http://dx.doi.org/10.1039/b900753a.

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49

SASAKI, Ren, Arif Md Rashedul KABIR, and Akira KAKUGO. "Biomolecular Motor Modulates Mechanical Property of Microtubules." Seibutsu Butsuri 55, no. 5 (2015): 259–61. http://dx.doi.org/10.2142/biophys.55.259.

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50

Kabir, Arif Md Rashedul, Daisuke Inoue, Yoshimi Hamano, Hiroyuki Mayama, Kazuki Sada, and Akira Kakugo. "Biomolecular Motor Modulates Mechanical Property of Microtubule." Biomacromolecules 15, no. 5 (April 23, 2014): 1797–805. http://dx.doi.org/10.1021/bm5001789.

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