9 research outputs found
Variable structure robot control systems: The RAPP approach
International audienceThis paper presents a method of designing variable structure control systems for robots. As the on-board robot computational resources are limited, but in some cases the demands imposed on the robot by the user are virtually limitless, the solution is to produce a variable structure system. The task dependent part has to be exchanged, however the task governs the activities of the robot. Thus not only exchange of some task-dependent modules is required, but also supervisory responsibilities have to be switched. Such control systems are necessary in the case of robot companions, where the owner of the robot may demand from it to provide many services.
Solution structure of biopolymers: a new method of constructing a bead model.
We propose a new, automated method of converting crystallographic data into a bead model used for the calculations of hydrodynamic properties of rigid macromolecules. Two types of molecules are considered: nucleic acids and small proteins. A bead model of short DNA fragments has been constructed in which each nucleotide is represented by two identical, partially overlapping spheres: one for the base and one for the sugar and phosphate group. The optimum radius sigma = 5.0 A was chosen on the basis of a comparison of the calculated translational diffusion coefficients (D(T)) and the rotational relaxation times (tau(R)) with the corresponding experimental data for B-DNA fragments of 8, 12, and 20 basepairs. This value was assumed for the calculation D(T) and tau(R) of tRNA(Phe). Better agreement with the experimental data was achieved for slightly larger sigma = 5.7 A. A similar procedure was applied to small proteins. Bead models were constructed such that each amino acid was represented by a single sphere or a pair of identical, partially overlapping spheres, depending on the amino acid's size. Experimental data of D(T) of small proteins were used to establish the optimum value of sigma = 4.5 A for amino acids. The lack of experimental data on tau(R) for proteins restricted the tests to the translational diffusion properties
High-pressure small-angle neutron scattering studies of glucose isomerase conformation in solution
Small-angle neutron scattering (SANS) of solutions of glucose/xylose isomerase from Streptomyces rubiginosus was measured as a function of pressure. It is shown that the structure of the enzyme in solution as seen by SANS is practically the same as that in the crystal and does not change with pressure up to 150 MPa. This reflects the unusually high structural stability of this material, which makes it extremely interesting to use as a secondary standard for pressure-dependent SANS experiments. This lack of pressure dependence of the SANS data also indicates that any possible change in hydration of the protein induced by pressure is not visible in the SANS curves. An appropriate correction procedure must be used for the SANS data in order to account for the distortion of the intensity curve due to hard-sphere and electrostatic interactions. After this correction, the isomerase can be readily used as a secondary standard for SANS measurements
Structure of the Intrinsically Disordered Protein Otholith in Solution at Different Protein and Salt Concentrations
Two members of the intrinsically disordered proteins (IDP) family (OMM-64 and STM) have been studied by means of small angle neutron scattering (SANS), dynamic light scattering (DLS) and fluorescence correlation spectroscopy (FCS). SANS curves of the proteins in D2O buffers have been measured for a range of Na+ and Ca2+ salts concentrations. The same samples have been measured using DLS in order to estimate their apparent hydrodynamic radii (Rh) and the scattering intensity in the q = 0 limit. The size of the proteins as a function of Na+ and Ca2+ concentrations had been measured in nano-molar concentrations using FCS. Fits to the SANS data suggest a coiled structure of the proteins in solution. For the first time SANS curves of proteins embedded in calcium carbonate crystals have been measured. Also a coiled structure has been found (slope = -2). Exact values of the radius of gyration (Rg) from SANS need measurements at smaller q-values
Nano-viscosity of supercooled liquid measured by fluorescence correlation spectroscopy: pressure and temperature dependence and the density scaling
The Stokes-Einstein relation allows us to calculate apparent viscosity experienced by tracers in complex media on the basis of measured self-diffusion coefficients. Such defined nano-viscosity values can be obtained through single particle techniques, like fluorescence correlation spectroscopy (FCS) and particle tracking (PT). In order to perform such measurements, as functions of pressure and temperature, a new sample cell was designed and is described in this work. We show that this cell in combination with a long working distance objective of the confocal microscope can be used for successful FCS, PT, and confocal imaging experiments in broad pressure (0.1-100 MPa) and temperature ranges. The temperature and pressure dependent nano-viscosity of a van der Waals liquid obtained from the translational diffusion coefficient measured in this cell by means of FCS obeys the same scaling as the rotational relaxation and macro-viscosity of the system