A molecular dynamics study of filamin repeat mechanics.
Published: 2006
Language: eng
Number of pages: 152
ISBN-13: 9780494210215
Description: The response of domains of the actin cross-linking protein filamin to mechanical stretching forces has recently been characterized by atomic force microscopy using both wildtype and mutant filamin domains. These mutations may have affected the mechanical behaviour of the filamin domain. To investigate the conclusions of this experimental study without resorting to mutations, we have used a computational approach called molecular dynamics. With respect to the sequence of mechanical unfolding events, computational results were more heterogeneous than the experiment implied, but we argue that this heterogeneity was likely an artefact of the computational approach, and that the conclusions of the experimentalists were most likely correct. In a related line of investigation, we have performed a preliminary characterization of the response of a pair of domains to forces that rotate one domain relative to the other, and we have found that such rotation can occur without distortion of the domains.
Notes: Source: Masters Abstracts International, Volume: 45-03, page: 1553.

Thesis (M.A.Sc.)--University of Toronto, 2006.

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