Two-stimuli manipulation of a biological motor.
Ristic, Zorica; Vitali, Marco; Duci, Alessandro; Goetze, Christian; Kemnitz, Klaus; Zuschratter, Werner; Lill, Holger; Bald, Dirk.
; 7: 3, 2009 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-19445679
Dissecting the role of the Î³-subunit in the rotary-chemical coupling and torque generation of F1-ATPase.
Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer.
Rotary catalysis of the stator ring of F(1)-ATPase.
Mechanochemical Energy Transduction during the Main Rotary Step in the Synthesis Cycle of F<sub>1</sub>-ATPase.
Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase.
Robustness of the rotary catalysis mechanism of F1-ATPase.
Single-molecule analysis of the rotation of F1-ATPase under high hydrostatic pressure.
Torque, chemistry and efficiency in molecular motors: a study of the rotary-chemical coupling in F1-ATPase.
Effect of the MotA(M206I) Mutation on Torque Generation and Stator Assembly in the <i>Salmonella</i> H<sup>+</sup>-Driven Flagellar Motor.
In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.