Abstract

At scales below micrometers, Brownian motion dictates most of the behaviors. The simple observation of a colloid is striking: a permanent and random motion is seen, whereas inertial forces play a negligible role. This Physics, where velocity is proportional to force, has opened new horizons in biology. The random feature is challenged in living systems where some proteins - molecular motors - have a directed motion whereas their passive behaviors of colloid should lead to a Brownian motion. Individual proteins, polymers of living matter such as DNA, RNA, actin or microtubules, molecular motors, all these objects can be viewed as chains of colloids. They are submitted to shocks from molecules of the solvent. Shapes taken by these biopolymers or dynamics imposed by motors can be measured and modeled from single molecules to their collective effects. Thanks to the development of experimental methods such as optical tweezers, Atomic Force Microscope (AFM), micropipettes, and quantitative fluorescence (such as Förster Resonance Energy Transfer, FRET), it is possible to manipulate these individual biomolecules in an unprecedented manner: experiments allow to probe the validity of models; and a new Physics has thereby emerged with original biological insights. Theories based on statistical mechanics are needed to explain behaviors of these systems. When force-extension curves of these molecules are extracted, the curves need to be fitted with models that predict the deformation of free objects or submitted to a force. When velocity of motors is altered, a quantitative analysis is required to explain the motions of individual molecules under external forces. This lecture will give some elements of introduction to the lectures of the session 'Nanophysics for Molecular Biology'.

Highlights

  • A word of a caution about the style adopted in this review

  • I start by giving basic ideas and estimates for the Physics associated with single molecules; I continue by presenting simple ideas in the Physics of single polymers

  • The hydrolysis of Adenosine Tri-Phosphate (ATP) is of the order of 10kBT; the binding energy of the motor to the filament is of the order of 10kBT - allowing the couple motor-track to ‘resist’ to Brownian motion with a lower energy, kBT

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Summary

Introduction

A word of a caution about the style adopted in this review. The goal is not to present a formal lecture. Forces applied to single molecules allow the evaluation of binding interactions between domains in single proteins or between motors and their partners Their dynamics of opening or their rules for stabilities or assembly and disassembly can be predicted in a quantitative manner. Molecular motors: experiments and theory As we said before, colloids or single molecules undergo a random motion This motion can be rectified, i.e. with a source of energy usually associated with the hydrolysis of ATP/GTP, a molecule can move directionally along a track. When the myosin has an elementary step in one direction, its amplitude a is known to be of the order of 1 nm These scales of energy and length allow to set the typical force F associated with single motors. Such approaches have suggested that collective effects can be critically important for morphogenesis [12]

Conclusions
Howard J
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