By Masahiro Kinoshita
This short discusses the mechanism of sensible expression of a protein or protein advanced using the ATP hydrolysis cycle or proton-motive strength from a distinct standpoint interested in the jobs of water. various tactics are thought of equivalent to the unidirectional circulation of a linear-motor protein alongside a filament, insertion of an spread out protein right into a chaperonin and unlock of the folded protein from it, delivery of various substrates around the membrane by way of a transporter, and directed rotation of the principal subunit inside of a rotatory motor protein advanced. those issues are mentioned in a unified demeanour in the comparable theoretical framework. the writer argues that water performs primary roles within the useful expression of those molecular machines. A pivotal issue is the entropic strength or power originating from the translational displacement of water molecules coexisting with the molecular machines within the whole system.
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Additional resources for Mechanism of Functional Expression of the Molecular Machines
When ATP binds to myosin, tight packing of myosin and ATP occurs and the myosin structure undergoes a large change. As a result, the packing of myosin and F-actin is inevitably loosened. ) We assume as an approximation that myosin takes only two distinct geometries: one of them is in states 2 and 3 and the other is in states 1, 4, and 5. 3). We model S1 in states 1, 4, and 5 as a large hard sphere with diameter dB (geometry 1) and S1 in states 2 and 3 as a large hard sphere with diameter dB possessing a cleft on the S1/F-actin interface (geometry 2).
28 nm). The solute I-solvent (I = 1, 2) interaction potential is taken to be uIS(h) = ∞ for h < dS/2, where h is the distance between the center of a small sphere and the nearest surface of solute I. In uIS(h) for h > dS/2, which includes an important parameter ξI (>0), the repulsive part of the 9–3 type potential is simply replaced by a hard-core interaction and the potential at large separations is truncated . As ξI increases, the attractive part of uIS(h) becomes stronger. 5 for T = 298 K), and ξ1 and dB are varied as major parameters.
Subunit) of the α3β3γ complex taken from F1-ATPase has been shown to exhibit a directed rotation. The α3β3γ complex is the most fundamental unit best suited to the investigation of the rotational mechanism of a rotary motor. 12. By utilizing the ATP hydrolysis cycle, the γ subunit rotates in a counterclockwise direction when viewed from the Fo side. We discuss the rotation mechanism with the emphasis on the water-entropy effect. 13a). ATP is bound to the β subunit named βTP. ATP is also bound to the β subunit named βDP, but ATP within βDP is ready to be hydrolyzed into ADP+Pi.