Skip to Main Content
 

Global Search Box

 
 
 
 

Files

File List


ucin1267737157.pdf (1.14 MB)

ETD Abstract Container

Abstract Header

Computer Simulations of Resilin-like Peptides

Petrenko, Roman
http://rave.ohiolink.edu/etdc/view?acc_num=ucin1267737157

Abstract Details

2010, PhD, University of Cincinnati, Arts and Sciences : Physics.
Resilin is an elastomeric protein characterized by rubber-like elasticity, very high resilience and high fatigue lifetime. These outstanding material properties are conferred by multiple elastic repeats, similar to those found in other elastomeric proteins. In this thesis I use molecular dynamics to elucidate the effect of amino-acid sequence variation on the mechanical properties of resilin-like peptides. In particular, I address the role of disorder in the relaxed (unstretched) state and the amount of conformational entropy lost upon extension. I simulate model systems comprising multiple identical repeats from single elastic units observed in fruit fly and mosquito resilin gene products. The length of the simulated peptides ranges from 11 to 176 residues. In order to study the nature of the restoring force in resilin I use steered molecular dynamics (SMD) and fixed end simulations. I find a high level of disorder and lack of stable secondary structure for the well solvated relaxed state in all simulated peptides; these results are consistent with conclusions from circular dichroism spectra of resilin-like peptides. Structural parameters, computed from molecular dynamics trajectories, are compared with experimental NMR and SAXS results. While upon stretching the conformational entropy is significantly decreased, the enthalpy is estimated to remain essentially unchanged. I conclude that the restoring force is primarily of entropic origin and largely insensitive to the amino-acid composition of resilin-like elastic repeats. Finally, I build a coarse-grained model from all-atomic simulation of two repeats in mosquito resilin and apply it larger peptides in order to assess flexibility and the effect of cross-linking in multiple resilin-like polypeptides.
Thomas Beck, PhD (Committee Chair)
Jaroslaw Meller, PhD (Committee Member)
Rostislav Serota, PhD (Committee Member)
107 p.
Biophysics
resilin-like peptides; resilin; entropic force; rubber-like elasticity; conformational entropy; molecular dynamics

Recommended Citations

Citations

  • Petrenko, R. (2010). Computer Simulations of Resilin-like Peptides [Doctoral dissertation, University of Cincinnati]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1267737157

    APA Style (7th edition)

  • Petrenko, Roman. Computer Simulations of Resilin-like Peptides. 2010. University of Cincinnati, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=ucin1267737157.

    MLA Style (8th edition)

  • Petrenko, Roman. "Computer Simulations of Resilin-like Peptides." Doctoral dissertation, University of Cincinnati, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1267737157

    Chicago Manual of Style (17th edition)

ucin1267737157
717
© 2010, some rights reserved.Creative Commons License Computer Simulations of Resilin-like Peptides by Roman Petrenko is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. Based on a work at etd.ohiolink.edu.
This open access ETD is published by University of Cincinnati and OhioLINK.