ArticleBiophysical journal2003
The force-driven conformations of heparin studied with single molecule force microscopy.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 48 citations in OpenAlex.
- Engineering Host-Guest Interactions for Next-Generation Heparin Biosensors.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Article
- The Role of Single-Molecule Force Spectroscopy in Unraveling Typical and Autoimmune Heparin-induced Thrombocytopenia.International journal of molecular sciences · 2018Review
- Velocity-dependent mechanical unfolding of bacteriorhodopsin is governed by a dynamic interaction network.Biophysical journal · 2011Article
- Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Equilibrium sampling for biomolecules under mechanical tension.Biophysical journal · 2010Article
- Mechanical stability of helical beta-peptides and a comparison of explicit and implicit solvent models.Biophysical journal · 2008Article
- Direct detection of the formation of V-amylose helix by single molecule force spectroscopy.Journal of the American Chemical Society · 2006Article
- Molecular dynamics simulations of forced conformational transitions in 1,6-linked polysaccharides.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.