title: Influence of architecture on the kinetic stability of molecular assemblies.
abstract: The strength of a multimolecular system depends on the number of interactions that hold it together. Using dynamic force spectroscopy, we show how the kinetic stability of a system decreases as the number of molecular bonds is increased, as predicted by theory. The data raise important considerations for experimental tests of bond strength and, as a paradigm, suggest both routes to and pitfalls in methods for computational simulation of molecular transitions, such as ligand binding and protein folding.
authors.affiliation: Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, UK.
authors.forename: Amesh B
authors.initials: AB
authors.lastname: Patel
authors.forename: Stephanie
authors.initials: S
authors.lastname: Allen
authors.forename: Martyn C
authors.initials: MC
authors.lastname: Davies
authors.forename: Clive J
authors.initials: CJ
authors.lastname: Roberts
authors.forename: Saul J B
authors.initials: SJ
authors.lastname: Tendler
authors.forename: Philip M
authors.initials: PM
authors.lastname: Williams
mesh_terms: D001710:Biotin / Q000031:analogs & derivatives* / Q000737:chemistry*; D007700:Kinetics; D046911:Macromolecular Substances; D018625:Microscopy, Atomic Force; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D046911:Macromolecular Substances; D012710:Serum Albumin, Bovine; D001710:Biotin; C028072:2-iminobiotin