What is the biological relevance of the specific bond properties revealed by single-molecule studies?

During the last decade, many authors took advantage of new methodologies based on atomic force microscopy (AFM), biomembrane force probes (BFPs), laminar flow chambers or optical traps to study at the single‐molecule level the formation and dissociation of bonds between receptors and ligands attache...

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Bibliographic Details
Published in:Journal of molecular recognition 2007-11, Vol.20 (6), p.432-447
Main Authors: Robert, Philippe, Benoliel, Anne-Marie, Pierres, Anne, Bongrand, Pierre
Format: Article
Language:English
Subjects:
atomic force microscopy
Bell's law
Binding Sites - physiology
binding strength
Biochemistry, Molecular Biology
Biological Physics
biomembrane force probe
Biophysics
Computer Simulation
Hydrogen Bonding
Kinetics
laminar flow chamber
Life Sciences
Microscopy, Atomic Force - methods
Models, Biological
Models, Theoretical
off-rate
on-rate
optical traps
Physics
Protein Binding - physiology
Protein Interaction Mapping - methods
Protein Interaction Mapping - trends
Protein Structure, Secondary - physiology
Reproducibility of Results
surface-attached molecules
unbinding force
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Summary:During the last decade, many authors took advantage of new methodologies based on atomic force microscopy (AFM), biomembrane force probes (BFPs), laminar flow chambers or optical traps to study at the single‐molecule level the formation and dissociation of bonds between receptors and ligands attached to surfaces. Experiments provided a wealth of data revealing the complexity of bond response to mechanical forces and the dependence of bond rupture on bond history. These results supported the existence of multiple binding states and/or reaction pathways. Also, single bond studies allowed us to monitor attachments mediated by a few bonds. The aim of this review is to discuss the impact of this new information on our understanding of biological molecules and phenomena. The following points are discussed: (i) which parameters do we need to know in order to predict the behaviour of an encounter between receptors and ligands, (ii) which information is actually yielded by single‐molecule studies and (iii) is it possible to relate this information to molecular structure? Copyright © 2007 John Wiley & Sons, Ltd.
ISSN:0952-3499
1099-1352
DOI:10.1002/jmr.827