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Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1

[+] Author Affiliations
Liang Ma, Meixiang Xu, Andres F. Oberhauser

University of Texas Medical Branch, Galveston, TX

Paper No. NEMB2010-13093, pp. 365-366; 2 pages
doi:10.1115/NEMB2010-13093
From:
  • ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology
  • ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology
  • Houston, Texas, USA, February 7–10, 2010
  • Conference Sponsors: ASME Nanotechnology Council
  • ISBN: 978-0-7918-4392-5 | eISBN: 978-0-7918-3866-2
  • Copyright © 2010 by ASME

abstract

The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells is the result of cycles of mechano-sensing, mechano-transduction, and mechano-response. Recently developed single-molecule atomic force microscopy (AFM) techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins, such as titin (an elastic mechano-sensing protein found in muscle) and polycystin-1 (PC1, a mechanosensor found in the kidney).

Copyright © 2010 by ASME

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