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Protein Molecules as Natural Nano Bio Devices: Mobility Analysis

[+] Author Affiliations
Zahra Shahbazi, Horea T. Ilieş, Kazem Kazerounian

University of Connecticut, Storrs, CT

Paper No. NEMB2010-13021, pp. 187-188; 2 pages
doi:10.1115/NEMB2010-13021
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

Proteins are nature’s nano-robots in the form of functional molecular components of living cells. The function of these natural nano-robots often requires conformational transitions between two or more native conformations that are made possible by the intrinsic mobility of the proteins. Understanding these transitions is essential to the understanding of how proteins function, as well as to the ability to design and manipulate protein-based nano-mechanical systems [1]. Modeling protein molecules as kinematic chains provides the foundation for developing powerful approaches to the design, manipulation and fabrication of peptide based molecules and devices. Nevertheless, these models possess a high number of degrees of freedom (DOF) with considerable computational implications. On the other hand, real protein molecules appear to exhibits a much lower mobility during the folding process than what is suggested by existing kinematic models. The key contributor to the lower mobility of real proteins is the formation of Hydrogen bonds during the folding process.

Copyright © 2010 by ASME

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