help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published August 12, 2005. doi:10.1529/biophysj.105.061606
© 2005 by the Biophysical Society.

A more recent version of this article appeared on November 1, 2005.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.105.061606v1
89/5/3434    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hukkanen, E.
Right arrow Articles by Braatz, R. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hukkanen, E.
Right arrow Articles by Braatz, R. D.

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




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Q. Shi, Y.-H. Chien, and D. Leckband
Biophysical Properties of Cadherin Bonds Do Not Predict Cell Sorting
J. Biol. Chem., October 17, 2008; 283(42): 28454 - 28463.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. Guo, C. Ray, A. Kirkpatrick, N. Lad, and B. B. Akhremitchev
Effects of Multiple-Bond Ruptures on Kinetic Parameters Extracted from Force Spectroscopy Measurements: Revisiting Biotin-Streptavidin Interactions
Biophys. J., October 15, 2008; 95(8): 3964 - 3976.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. Yersin, T. Osada, and A. Ikai
Exploring Transferrin-Receptor Interactions at the Single-Molecule Level
Biophys. J., January 1, 2008; 94(1): 230 - 240.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. A. Wieland, A. A. Gewirth, and D. E. Leckband
Single Molecule Adhesion Measurements Reveal Two Homophilic Neural Cell Adhesion Molecule Bonds with Mechanically Distinct Properties
J. Biol. Chem., December 9, 2005; 280(49): 41037 - 41046.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2005 by the Biophysical Society.