14
1 Brownian Ratchets and Molecular Motors
35. Kramers, H.A.: Brownian motion in a field of force and the diffusion model of chemical
reactions. Physica 7, 284–304 (1940)
36. Yasuda, R., Noji, H., Kinosita, K., Yoshida, M.: F1-ATPase is a highly efficient molecular
motor that rotates with discrete 120 ◦ steps. Cell 93, 1117 (1998)
37. Noji, H., Yasuda, R., Yoshida, M., Kinosita, K.: Direct observation of the rotation of F1ATPase. Nature 386, 299 (1997)
38. Howard, J.: Protein power strokes. Curr. Biol. 16(14), R517–R519 (2006)
39. Cooke, R.: The mechanism of muscle contraction. CRC Crit. Rev. Biochem. 21, 53–118 (1986)
40. Hwang, W., Karplus, M.: Structural basis for power stroke vs. Brownian ratchet mechanisms
of motor proteins. Proc. Natl. Acad. Sci. U. S. A. 116(40), 19777–19785 (2019)
41. Yang, W., Gao, Y.Q., Cui, Q., Ma, J., Karplus, M.: The missing link between thermodynamics
and structure in F1-ATPase. Proc. Natl. Acad. Sci. U. S. A. 100, 874–879 (2003)
42. Gao, Y.Q., Yang, W., Karplus, M.: A structure-based model for the synthesis and hydrolysis of
ATP by F1-ATPase. Cell 123, 195–205 (2005)
43. Pu, J., Karplus, M.: How subunit coupling produces the γ -subunit rotary motion in F1-ATPase.
Proc. Natl. Acad. Sci. U. S. A. 105, 1192–1197 (2008)
44. Nam, K., Pu, J., Karplus, M.: Trapping the ATP binding state leads to a detailed understanding
of the F1-ATPase mechanism. Proc. Natl. Acad. Sci. U. S. A. 111, 17851–17856 (2014)
45. Bason, J.V., Montgomery, M.G., Leslie, A.G.W., Walker, J.E.: How release of phosphate from
mammalian F1-ATPase generates a rotary substep. Proc. Natl. Acad. Sci. U. S. A. 112, 6009–
6014 (2015)
1 Brownian Ratchets and Molecular Motors
35. Kramers, H.A.: Brownian motion in a field of force and the diffusion model of chemical
reactions. Physica 7, 284–304 (1940)
36. Yasuda, R., Noji, H., Kinosita, K., Yoshida, M.: F1-ATPase is a highly efficient molecular
motor that rotates with discrete 120 ◦ steps. Cell 93, 1117 (1998)
37. Noji, H., Yasuda, R., Yoshida, M., Kinosita, K.: Direct observation of the rotation of F1ATPase. Nature 386, 299 (1997)
38. Howard, J.: Protein power strokes. Curr. Biol. 16(14), R517–R519 (2006)
39. Cooke, R.: The mechanism of muscle contraction. CRC Crit. Rev. Biochem. 21, 53–118 (1986)
40. Hwang, W., Karplus, M.: Structural basis for power stroke vs. Brownian ratchet mechanisms
of motor proteins. Proc. Natl. Acad. Sci. U. S. A. 116(40), 19777–19785 (2019)
41. Yang, W., Gao, Y.Q., Cui, Q., Ma, J., Karplus, M.: The missing link between thermodynamics
and structure in F1-ATPase. Proc. Natl. Acad. Sci. U. S. A. 100, 874–879 (2003)
42. Gao, Y.Q., Yang, W., Karplus, M.: A structure-based model for the synthesis and hydrolysis of
ATP by F1-ATPase. Cell 123, 195–205 (2005)
43. Pu, J., Karplus, M.: How subunit coupling produces the γ -subunit rotary motion in F1-ATPase.
Proc. Natl. Acad. Sci. U. S. A. 105, 1192–1197 (2008)
44. Nam, K., Pu, J., Karplus, M.: Trapping the ATP binding state leads to a detailed understanding
of the F1-ATPase mechanism. Proc. Natl. Acad. Sci. U. S. A. 111, 17851–17856 (2014)
45. Bason, J.V., Montgomery, M.G., Leslie, A.G.W., Walker, J.E.: How release of phosphate from
mammalian F1-ATPase generates a rotary substep. Proc. Natl. Acad. Sci. U. S. A. 112, 6009–
6014 (2015)