Force-induced deformations and stability of biological bonds.
A deformation model of the forced-induced dissociation of biological bonds is developed. A simple illustration shows that protein deformations can change the receptor-ligand interaction linearly with applied force at small forces, either increasing or decreasing the bond stability, and that a minor external work can lead to notable changes in the interaction energy. The deformation-induced increase of bond stability is illustrated with the remarkable catch-bond phenomenon in P and L selections. Additionally, the model rationalizes the frequently seen disparity between the bond dissociation rates of many free complexes and the zero-force asymptotic rates measured by force spectroscopy.
Pereverzev
Yuriy V
YV
Department of Chemistry, University of Washington, Seattle, Washington 98195-1700, USA.
Prezhdo
Oleg V
OV
D001665:Binding Sites; D001704:Biopolymers / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D018625:Microscopy, Atomic Force / Q000379:methods*; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D010812:Physical Stimulation; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D013314:Stress, Mechanical
D001704:Biopolymers; D011506:Proteins