By Mustapha Hamdi
Nanorobots characterize a nanoscale equipment the place proteins reminiscent of DNA, carbon nanotubes may possibly act as vehicles, mechanical joints, transmission components, or sensors. while those diversified parts have been assembled jointly they could shape nanorobots with multi-degree-of-freedom, in a position to observe forces and manage items within the nanoscale global. Design, Modeling and Characterization of Bio-Nanorobotic platforms investigates the layout, meeting, simulation, and prototyping of organic and synthetic molecular buildings with the target of enforcing their inner nanoscale activities inside of nanorobotic structures in an optimized manner.
Design, Modeling and Characterization of Bio-Nanorobotic Systems focuses, generally on methods. the 1st one consists of multiscale modeling instruments (quantum mechanics, molecular dynamics, continuum mechanics) coupled to digital fact complicated ideas. so that it will layout and overview the features of molecular robots, we proposed interactive nanophysics-based simulation which allows manipulation of molecules, proteins and engineered fabrics in molecular dynamics simulations with real-time strength suggestions and graphical demonstrate. the second one process makes use of a unique co-prototyping technique, the place the nanorobotic’s multiscale version is coupled to experimental measurements.
Design, Modeling and Characterization of Bio-Nanorobotic Systems offers a unique proposal of nanorobots, bio-nanoactuators established DNA and rotating nanodevices dependent carbon nanotubes. moreover the offered platform helped to symbolize the interplay among novel drug supply platforms and mobile membrane.
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Extra resources for Design, Modeling and Characterization of Bio-Nanorobotic Systems
It is one of the few cases in which structure can reliably be predicted from sequence. 2. Triple-stranded helix tropocollagen protein: Although the amino acid proline, which lacks an N–H group, is not frequently found in an alpha helix, two interesting helical structures can be formed from sequences rich in proline residues. The first is the collagen triple helix (Fig. 9). Collagen is the main constituent of the bones, tendons, ligaments and blood vessels of higher organisms and consists of a repeating tripeptide in which every third residue is a glycine (GlyXY)n.
10). Nearly all polar amide groups are hydrogen bonded to one another in a beta-sheet structure, except for the N–H and C=O groups on the outer sides of the two edge strands. Edge strands may make hydrogen bonds in any of several ways. They may simply make hydrogen bonds to water, if they are exposed to solvent; or they may pack against polar side chains in, for example, a neighboring alpha helix; or they may make hydrogen bonds to an edge strand in another protein chain, forming an extended beta structure that spans more than one subunit and thereby stabilizes quaternary structure (Fig.
The macrocycle encircles the thread-like portion of the dumb-bell with heavy groups at its ends. The thread has two recognition sites which can be altered reversibly so as to make the macrocycle shuttle between the two sites  24 1 Current State-of-the-Art on Nanorobotic Components and Design be chemical, electrochemical or photochemical [127, 128]. The stereo-electronic properties of the recognition sites can be altered protonation or deprotonation, or by oxidation or reduction, thereby changing their affinity towards the macrocycle.