Influence of architecture on the kinetic stability of molecular assemblies.
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.
Patel
Amesh B
AB
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, UK.
Allen
Stephanie
S
Davies
Martyn C
MC
Roberts
Clive J
CJ
Tendler
Saul J B
SJ
Williams
Philip M
PM
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
D046911:Macromolecular Substances; D012710:Serum Albumin, Bovine; D001710:Biotin; C028072:2-iminobiotin