Strength of a weak bond connecting flexible polymer chains - PubMed (original) (raw)
Strength of a weak bond connecting flexible polymer chains
E Evans et al. Biophys J. 1999 May.
Abstract
Bond dissociation under steadily rising force occurs most frequently at a time governed by the rate of loading (Evans and Ritchie, 1997 Biophys. J. 72:1541-1555). Multiplied by the loading rate, the breakage time specifies the force for most frequent failure (called bond strength) that obeys the same dependence on loading rate. The spectrum of bond strength versus log(loading rate) provides an image of the energy landscape traversed in the course of unbonding. However, when a weak bond is connected to very compliant elements like long polymers, the load applied to the bond does not rise steadily under constant pulling speed. Because of nonsteady loading, the most frequent breakage force can differ significantly from that of a bond loaded at constant rate through stiff linkages. Using generic models for wormlike and freely jointed chains, we have analyzed the kinetic process of failure for a bond loaded by pulling the polymer linkages at constant speed. We find that when linked by either type of polymer chain, a bond is likely to fail at lower force under steady separation than through stiff linkages. Quite unexpectedly, a discontinuous jump can occur in bond strength at slow separation speed in the case of long polymer linkages. We demonstrate that the predictions of strength versus log(loading rate) can rationalize conflicting results obtained recently for unfolding Ig domains along muscle titin with different force techniques.
Similar articles
- Model for stretching and unfolding the giant multidomain muscle protein using single-molecule force spectroscopy.
Staple DB, Payne SH, Reddin AL, Kreuzer HJ. Staple DB, et al. Phys Rev Lett. 2008 Dec 12;101(24):248301. doi: 10.1103/PhysRevLett.101.248301. Epub 2008 Dec 8. Phys Rev Lett. 2008. PMID: 19113678 - Modeling AFM-induced PEVK extension and the reversible unfolding of Ig/FNIII domains in single and multiple titin molecules.
Zhang B, Evans JS. Zhang B, et al. Biophys J. 2001 Feb;80(2):597-605. doi: 10.1016/S0006-3495(01)76040-7. Biophys J. 2001. PMID: 11159428 Free PMC article. - The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy.
Rief M, Gautel M, Schemmel A, Gaub HE. Rief M, et al. Biophys J. 1998 Dec;75(6):3008-14. doi: 10.1016/S0006-3495(98)77741-0. Biophys J. 1998. PMID: 9826620 Free PMC article. - Probing the relation between force--lifetime--and chemistry in single molecular bonds.
Evans E. Evans E. Annu Rev Biophys Biomol Struct. 2001;30:105-28. doi: 10.1146/annurev.biophys.30.1.105. Annu Rev Biophys Biomol Struct. 2001. PMID: 11340054 Review. - Protein unfolding and refolding under force: methodologies for nanomechanics.
Samorì B, Zuccheri G, Baschieri R. Samorì B, et al. Chemphyschem. 2005 Jan;6(1):29-34. doi: 10.1002/cphc.200400343. Chemphyschem. 2005. PMID: 15688640 Review.
Cited by
- Strong, tough, rapid-recovery, and fatigue-resistant hydrogels made of picot peptide fibres.
Xue B, Bashir Z, Guo Y, Yu W, Sun W, Li Y, Zhang Y, Qin M, Wang W, Cao Y. Xue B, et al. Nat Commun. 2023 May 4;14(1):2583. doi: 10.1038/s41467-023-38280-4. Nat Commun. 2023. PMID: 37142590 Free PMC article. - AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements.
Fernandez M, Shkumatov AV, Liu Y, Stulemeijer C, Derclaye S, Efremov RG, Hallet B, Alsteens D. Fernandez M, et al. Nucleic Acids Res. 2023 Jun 9;51(10):4929-4941. doi: 10.1093/nar/gkad241. Nucleic Acids Res. 2023. PMID: 37026471 Free PMC article. - Low cost and massively parallel force spectroscopy with fluid loading on a chip.
Akbari E, Shahhosseini M, Robbins A, Poirier MG, Song JW, Castro CE. Akbari E, et al. Nat Commun. 2022 Nov 10;13(1):6800. doi: 10.1038/s41467-022-34212-w. Nat Commun. 2022. PMID: 36357383 Free PMC article. - The molecular mechanisms underlying mussel adhesion.
Li Y, Cao Y. Li Y, et al. Nanoscale Adv. 2019 Oct 10;1(11):4246-4257. doi: 10.1039/c9na00582j. eCollection 2019 Nov 5. Nanoscale Adv. 2019. PMID: 36134404 Free PMC article. Review. - Optimal Sacrificial Domains in Mechanical Polyproteins: S. epidermidis Adhesins Are Tuned for Work Dissipation.
Liu H, Liu Z, Yang B, Lopez Morales J, Nash MA. Liu H, et al. JACS Au. 2022 May 18;2(6):1417-1427. doi: 10.1021/jacsau.2c00121. eCollection 2022 Jun 27. JACS Au. 2022. PMID: 35783175 Free PMC article.
References
- Science. 1997 May 16;276(5315):1090-2 - PubMed
- Nature. 1997 May 15;387(6630):308-12 - PubMed
- Phys Rev Lett. 1996 Dec 30;77(27):5389-5392 - PubMed
- Nature. 1998 May 14;393(6681):181-5 - PubMed
- Biophys J. 1995 Jun;68(6):2580-7 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources