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Biophys. J. BioFAST: First Published August 12, 2005. doi:10.1529/biophysj.105.061606
© 2005 by the Biophysical Society.

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SPECTROSCOPY, IMAGING, OTHER TECHNIQUES

Multiple-Bond Kinetics from Single-Molecule Pulling Experiments: Evidence for Multiple NCAM Bonds

Eric Hukkanen 1, Julie Wieland 2, Andrew Gewirth 1, Deborah Leckband 1* and Richard D. Braatz 1

1 University of Illinois
2 University of Ilinois

* To whom correspondence should be addressed. E-mail: leckband{at}uiuc.edu.

Submitted on February 20, 2005
Revised on April 15, 2005
Accepted on 8 July 2005


  Abstract
The kinetic parameters of single bonds between neural cell adhesion molecules were determined from atomic force microscope measurements of the forced dissociation of homophilic protein-protein bonds. The analysis of the bond rupture data at different loading rates, using the single-bond full microscopic model, indicates that the breakage frequency distribution is most sensitive to the distance to the transition state and least sensitive to the molecular spring constant. The described analytical approach also provides a systematic procedure for obtaining bond rutpure kinetics for single protein bonds from bond breakage frquency distributions obtained from single-molecule pulling experiments. In this case, the analysis of neural cell adhesion molecule bond failure measurements motivates the use of a double-bond microscopic model that requires an additional kinetic parameter. This double-bond microscopic model, which assumes two independent boudn states, more accurately describes the breakage frequency distribution, particularly at high loading rates. This finding agrees with recent surface force measurements, which showed that the neural cell adhesion molecule forms two spatially distinct bonds between opposed proteins.

Key Words: NCAM, atomic force microscope, bond rupture, cumulative distribution, multivariate statistics, single molecule




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Copyright © 2005 by the Biophysical Society.