Thermal fluctuations biased for directional motion in molecular motors.
Recently developed single molecule measurements have demonstrated that the mechanisms for numerous protein functions involve thermal fluctuation, or Brownian motion. Protein interactions bias the random thermal noise in a manner such that the protein can perform its given functions. This phenomenon has been observed in molecular motor unidirectional movement where Brownian motion is used to preferentially bind the motor heads in one direction causing directional motility. This is analogous to that used by proteins in which spontaneous structural fluctuations are used to switch function. Seeing that two very different systems implement similar mechanisms suggests there exists a general scheme applied by diverse proteins that exploits thermal fluctuations in order to achieve their respective functions.
Ishii
Yoshiharu
Y
Formation of Soft Nano-Machines, CREST, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan. ishii@phys1.med.osaka-u.ac.jp
Taniguchi
Yuichi
Y
Iwaki
Mitsuhiro
M
Yanagida
Toshio
T
D031541:Fluorescence Resonance Energy Transfer; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000378:metabolism*; D009068:Movement; D018995:Myosin Heavy Chains / Q000378:metabolism; D011487:Protein Conformation; D013696:Temperature
D020409:Molecular Motor Proteins; C089785:myosin VI; D018995:Myosin Heavy Chains