Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase

Details Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase

2002-05-02

arxiv.org/abs/physics/0205005v1

Physics

Biological Physics

7 figures

Scientific paper

Two simple (rotator and one-particle) mechanistic models are suggested to describe simultaneously at a minimal level of sophistication two basic functions of F$_1$-ATPase: a motor regime driven by ATP hydrolysis and its inverted function as ATP synthesis. This description is consistent with the so-called rotary binding-change mechanism, a milestone of functioning ATP synthase, and uses a stepping (driving) function associated with two sequences of time instants, at which hydrolysis and synthesis reactions occur. It is useful to analyse experimental data and numerical simulations indeed predict corresponding dynamic behavior.

Affiliated with

Also associated with

No associations

Rating

Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-232414