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The force-driven conformations of heparin studied with single molecule force microscopy.

Publication ,  Journal Article
Marszalek, PE; Oberhauser, AF; Li, H; Fernandez, JM
Published in: Biophysical journal
October 2003

Using single molecule force spectroscopy we examine the response of heparin chains to mechanical stretching. We find that at forces below 200 pN heparin behaves as a simple entropic spring. At approximately 200 pN heparin displays a large enthalpic elasticity, which is evident as a pronounced plateau in the force-extension relationship. We determine that this enthalpic elasticity is produced by sugar rings of heparin flipping to more energetic and more extended conformations. We estimate that in vivo, the forces which stretch heparin are comparable to the forces that trigger conformational transitions in our single molecule atomic force microscopy measurements. We hypothesize that these conformational transitions have biological significance in that they provide a mechanism to finely regulate the affinity of various ligands toward heparin, for example, in secretory granules undergoing exocytosis and during the mechanical interactions between cells and the extracellular matrix.

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Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

October 2003

Volume

85

Issue

4

Start / End Page

2696 / 2704

Related Subject Headings

  • Stress, Mechanical
  • Physical Stimulation
  • Motion
  • Molecular Conformation
  • Models, Molecular
  • Microscopy, Atomic Force
  • Heparin
  • Elasticity
  • Computer Simulation
  • Biophysics
 

Citation

APA
Chicago
ICMJE
MLA
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Marszalek, P. E., Oberhauser, A. F., Li, H., & Fernandez, J. M. (2003). The force-driven conformations of heparin studied with single molecule force microscopy. Biophysical Journal, 85(4), 2696–2704. https://doi.org/10.1016/s0006-3495(03)74692-x
Marszalek, Piotr E., Andres F. Oberhauser, Hongbin Li, and Julio M. Fernandez. “The force-driven conformations of heparin studied with single molecule force microscopy.Biophysical Journal 85, no. 4 (October 2003): 2696–2704. https://doi.org/10.1016/s0006-3495(03)74692-x.
Marszalek PE, Oberhauser AF, Li H, Fernandez JM. The force-driven conformations of heparin studied with single molecule force microscopy. Biophysical journal. 2003 Oct;85(4):2696–704.
Marszalek, Piotr E., et al. “The force-driven conformations of heparin studied with single molecule force microscopy.Biophysical Journal, vol. 85, no. 4, Oct. 2003, pp. 2696–704. Epmc, doi:10.1016/s0006-3495(03)74692-x.
Marszalek PE, Oberhauser AF, Li H, Fernandez JM. The force-driven conformations of heparin studied with single molecule force microscopy. Biophysical journal. 2003 Oct;85(4):2696–2704.
Journal cover image

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

October 2003

Volume

85

Issue

4

Start / End Page

2696 / 2704

Related Subject Headings

  • Stress, Mechanical
  • Physical Stimulation
  • Motion
  • Molecular Conformation
  • Models, Molecular
  • Microscopy, Atomic Force
  • Heparin
  • Elasticity
  • Computer Simulation
  • Biophysics