2017/04/22 by Samuel Bell, Bell, Samuel, Eugene M. Terentjev +1
Biochemistry, Genetics and Molecular Biology · Medicine · Physics and Astronomy · #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Force Microscopy Techniques and Applications #Monoclonal and Polyclonal Antibodies Research #Protein purification and stability #Soft Condensed Matter (cond-mat.soft)
paper · pdf · doi:10.48550/arxiv.1704.06773
openalex publication_date 2017/04/22 · openalex created_date 2017/05/05 · openalex updated_date 2026/07/28
This paper considers a broadly biologically relevant question of a chain (such as a protein) binding to a sequence of receptors with matching multiple ligands distributed along the chain. This binding is critical in cell adhesion events, and in protein self-assembly. Using a mean field approximation of polymer dynamics, we first calculate the characteristic binding time for a tethered ligand reaching for a specific binding site on the surface. This time is determined by two separate entropic effects: an entropic barrier for the chain to be stretched sufficiently to reach the distant target, and a restriction on chain conformations near the surface. We then derive the characteristic time for a sequence of single binding events, and find that it is determined by the `zipper effect', optimizing the sequence of single and multiple binding steps.