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      Artificial molecular rotors and motors on surfaces: STM reveals and triggers

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      Soft Matter
      Royal Society of Chemistry (RSC)

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          Synthetic molecular motors and mechanical machines.

          The widespread use of controlled molecular-level motion in key natural processes suggests that great rewards could come from bridging the gap between the present generation of synthetic molecular systems, which by and large rely upon electronic and chemical effects to carry out their functions, and the machines of the macroscopic world, which utilize the synchronized movements of smaller parts to perform specific tasks. This is a scientific area of great contemporary interest and extraordinary recent growth, yet the notion of molecular-level machines dates back to a time when the ideas surrounding the statistical nature of matter and the laws of thermodynamics were first being formulated. Here we outline the exciting successes in taming molecular-level movement thus far, the underlying principles that all experimental designs must follow, and the early progress made towards utilizing synthetic molecular structures to perform tasks using mechanical motion. We also highlight some of the issues and challenges that still need to be overcome.
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            Direct observation of the rotation of F1-ATPase.

            Cells employ a variety of linear motors, such as myosin, kinesin and RNA polymerase, which move along and exert force on a filamentous structure. But only one rotary motor has been investigated in detail, the bacterial flagellum (a complex of about 100 protein molecules). We now show that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion. A central rotor of radius approximately 1 nm, formed by its gamma-subunit, turns in a stator barrel of radius approximately 5nm formed by three alpha- and three beta-subunits. F1-ATPase, together with the membrane-embedded proton-conducting unit F0, forms the H+-ATP synthase that reversibly couples transmembrane proton flow to ATP synthesis/hydrolysis in respiring and photosynthetic cells. It has been suggested that the gamma-subunit of F1-ATPase rotates within the alphabeta-hexamer, a conjecture supported by structural, biochemical and spectroscopic studies. We attached a fluorescent actin filament to the gamma-subunit as a marker, which enabled us to observe this motion directly. In the presence of ATP, the filament rotated for more than 100 revolutions in an anticlockwise direction when viewed from the 'membrane' side. The rotary torque produced reached more than 40 pN nm(-1) under high load.
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              Making molecular machines work.

              In this review we chart recent advances in what is at once an old and very new field of endeavour--the achievement of control of motion at the molecular level including solid-state and surface-mounted rotors, and its natural progression to the development of synthetic molecular machines. Besides a discussion of design principles used to control linear and rotary motion in such molecular systems, this review will address the advances towards the construction of synthetic machines that can perform useful functions. Approaches taken by several research groups to construct wholly synthetic molecular machines and devices are compared. This will be illustrated with molecular rotors, elevators, valves, transporters, muscles and other motor functions used to develop smart materials. The demonstration of molecular machinery is highlighted through recent examples of systems capable of effecting macroscopic movement through concerted molecular motion. Several approaches to illustrate how molecular motor systems have been used to accomplish work are discussed. We will conclude with prospects for future developments in this exciting field of nanotechnology.
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                Author and article information

                Journal
                SMOABF
                Soft Matter
                Soft Matter
                Royal Society of Chemistry (RSC)
                1744-683X
                1744-6848
                2012
                2012
                : 8
                : 35
                : 9053
                Article
                10.1039/c2sm26235e
                4abbb237-a9ce-4969-9054-8833c970e6e3
                © 2012
                History

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