Original Assignee ASCENTIA IMAGING Inc Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) ( en Inventor Edward Dowski Bradley Sissom Gregory Johnson Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Pending Application number EP13733703.6A Other languages German ( de) Info Publication number EP2801077A1 EP2801077A1 EP13733703.6A EP13733703A EP2801077A1 EP 2801077 A1 EP2801077 A1 EP 2801077A1 EP 13733703 A EP13733703 A EP 13733703A EP 2801077 A1 EP2801077 A1 EP 2801077A1 Authority EP European Patent Office Prior art keywords localization polarization coded code systems Prior art date Legal status (The legal status is an assumption and is not a legal conclusion. Google Patents Coded localization systems, methods and apparatus Google Patents EP2801077A1 - Coded localization systems, methods and apparatus In order to explain the rotation under that condition one should either suppose a shorter distance between subunit a and c subunits complex or assume interaction of more than two charged amino acids residues.EP2801077A1 - Coded localization systems, methods and apparatus Thus, for generally accepted structural parameters of ATP synthase, two-charge electrostatic interaction model does not permit rotation of the rotor if elastic properties of the central stalk are tougher than mentioned above. It is remarkable that rotation will take place only under condition when the elasticity (Young's) module of the central stalk (gamma subunit and other minor subunits) is less than 5.0 x 10(7)N/m(2). If membrane viscosity and elastic resistance were taken into account then the time of a whole turnover could rise up to 6.3 x 10(-3)s. The initial torque, which caused the rotation, was estimated as 3.7 pN nm and for this pattern the angular movement of c subunits complex could not physically have a period less than 10(-9)s. On the base of available experimental data it was shown that electrostatic interaction of two charged amino acids residues is able to supply quite enough energy for the rotation. In the present study the mutual protein movement in the membrane part of F(0)F(1)-ATP syntase has been analysed within the framework of rigid body mechanics. However, many parameters of this movement are still unknown. It was previously shown that the ring of membrane subunits rotates past a fixed subunit during catalytic cycle of the enzyme. The protein consists of a water-soluble F(1) and a transmembrane F(0) proton transporter part. ATP synthase catalyses the formation of ATP from ADP and P(i) and is powered by the diffusion of protons throughout membranes down the proton electrochemical gradient.
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