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Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides

Publication ,  Journal Article
Valiaev, A; Dong, WL; Schmidler, S; Clark, RL; Chilkoti, A; Zauscher, S
Published in: Journal of the American Chemical Society
August 20, 2008

We investigated the effect of temperature, ionic strength, solvent polarity, and type of guest residue on the force-extension behavior of single, end-tethered elastin-like polypeptides (ELPs), using single molecule force spectroscopy (SMFS). ELPs are stimulus-responsive polypeptides that contain repeats of the five amino acids Val-Pro-Gly-Xaa-Gly (VPGXG), where Xaa is a guest residue that can be any amino acid with the exception of proline. We fitted the force-extension data with a freely jointed chain (FJC) model which allowed us to resolve small differences in the effective Kuhn segment length distributions that largely arise from differences in the hydrophobic hydration behavior of ELP. Our results agree qualitatively with predictions from recent molecular dynamics simulations and demonstrate that hydrophobic hydration modulates the molecular elasticity for ELPs. Furthermore, our results show that SMFS, when combined with our approach for data analysis, can be used to study the subtleties of polypeptide-water interactions and thus provides a basis for the study of hydrophobic hydration in intrinsically unstructured biomacromolecules. © 2008 American Chemical Society.

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Published In

Journal of the American Chemical Society

DOI

ISSN

0002-7863

Publication Date

August 20, 2008

Volume

130

Issue

33

Start / End Page

10939 / 10946

Related Subject Headings

  • Water
  • Temperature
  • Solvents
  • Protein Conformation
  • Peptides
  • Osmolar Concentration
  • Molecular Weight
  • Models, Chemical
  • Microscopy, Atomic Force
  • Hydrophobic and Hydrophilic Interactions
 

Citation

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Valiaev, A., Dong, W. L., Schmidler, S., Clark, R. L., Chilkoti, A., & Zauscher, S. (2008). Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides. Journal of the American Chemical Society, 130(33), 10939–10946. https://doi.org/10.1021/ja800502h
Valiaev, A., W. L. Dong, S. Schmidler, R. L. Clark, A. Chilkoti, and S. Zauscher. “Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides.” Journal of the American Chemical Society 130, no. 33 (August 20, 2008): 10939–46. https://doi.org/10.1021/ja800502h.
Valiaev A, Dong WL, Schmidler S, Clark RL, Chilkoti A, Zauscher S. Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides. Journal of the American Chemical Society. 2008 Aug 20;130(33):10939–46.
Valiaev, A., et al. “Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides.” Journal of the American Chemical Society, vol. 130, no. 33, Aug. 2008, pp. 10939–46. Scopus, doi:10.1021/ja800502h.
Valiaev A, Dong WL, Schmidler S, Clark RL, Chilkoti A, Zauscher S. Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides. Journal of the American Chemical Society. 2008 Aug 20;130(33):10939–10946.
Journal cover image

Published In

Journal of the American Chemical Society

DOI

ISSN

0002-7863

Publication Date

August 20, 2008

Volume

130

Issue

33

Start / End Page

10939 / 10946

Related Subject Headings

  • Water
  • Temperature
  • Solvents
  • Protein Conformation
  • Peptides
  • Osmolar Concentration
  • Molecular Weight
  • Models, Chemical
  • Microscopy, Atomic Force
  • Hydrophobic and Hydrophilic Interactions