| Literature DB >> 19344994 |
Oscar Björnham1, Jeanna Bugaytsova, Thomas Borén, Staffan Schedin.
Abstract
The binding strength of the Helicobacter pylori adhesin-receptor complex BabA-ABO/Lewis b has been analyzed by means of dynamic force spectroscopy. High-resolution measurements of rupture forces were performed in situ on single bacterial cells, expressing the high-affinity binding BabA adhesin, by the use of force measuring optical tweezers. The resulting force spectra revealed the mechanical properties of a single BabA-Leb bond. It was found that the bond is dominated by one single energy barrier and that it is a slip-bond. The bond length and thermal off-rate were assessed to be 0.86+/-0.07 nm and 0.015+/-0.006 s(-1), respectively.Entities:
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Year: 2009 PMID: 19344994 DOI: 10.1016/j.bpc.2009.03.007
Source DB: PubMed Journal: Biophys Chem ISSN: 0301-4622 Impact factor: 2.352