Dynamic force spectroscopy on soft molecular systems: Improved analysis of unbinding spectra with varying linker compliance
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Dynamic force spectroscopy on soft molecular systems : Improved analysis of unbinding spectra with varying linker compliance. / Thormann, Esben; Hansen, Per Lyngs; Simonsen, Adam Cohen; Mouritsen, Ole G.
In: Colloids and Surfaces B: Biointerfaces, Vol. 53, No. 2, 01.12.2006, p. 149-156.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Dynamic force spectroscopy on soft molecular systems
T2 - Improved analysis of unbinding spectra with varying linker compliance
AU - Thormann, Esben
AU - Hansen, Per Lyngs
AU - Simonsen, Adam Cohen
AU - Mouritsen, Ole G.
PY - 2006/12/1
Y1 - 2006/12/1
N2 - Dynamic force spectroscopy makes it possible to measure the breaking of single molecular bonds or the unfolding of single proteins subjected to a time-dependent pulling force. The force needed to break a single bond or to unfold a domain in a protein depends critically on the time dependence of the applied force. In this way the elastic response couples to the unbinding force. We have performed an experimental and theoretical examination of this coupling by studying the well-known biotin-streptavidin bond in systems incorporating two common types of linkers. In the first case biotin is linked by bovine serum albumin (BSA) and it is observed that this linker has a linear elastic response. More surprisingly we find that its force constant varies significantly between repeated force curves. It is demonstrated that by sorting the force curves according to the force constant of the linker we can improve the data analysis and obtain a better agreement between experimental data and theory. In the second case biotin is linked by poly(ethylene glycol) (PEG), which has a soft nonlinear elastic response. A numerical calculation of the unbinding statistics for the polymer system agrees quantitatively with experiments. It demonstrates a clear decrease in unbinding forces resulting from the polymer linker.
AB - Dynamic force spectroscopy makes it possible to measure the breaking of single molecular bonds or the unfolding of single proteins subjected to a time-dependent pulling force. The force needed to break a single bond or to unfold a domain in a protein depends critically on the time dependence of the applied force. In this way the elastic response couples to the unbinding force. We have performed an experimental and theoretical examination of this coupling by studying the well-known biotin-streptavidin bond in systems incorporating two common types of linkers. In the first case biotin is linked by bovine serum albumin (BSA) and it is observed that this linker has a linear elastic response. More surprisingly we find that its force constant varies significantly between repeated force curves. It is demonstrated that by sorting the force curves according to the force constant of the linker we can improve the data analysis and obtain a better agreement between experimental data and theory. In the second case biotin is linked by poly(ethylene glycol) (PEG), which has a soft nonlinear elastic response. A numerical calculation of the unbinding statistics for the polymer system agrees quantitatively with experiments. It demonstrates a clear decrease in unbinding forces resulting from the polymer linker.
KW - AFM
KW - Biotin-streptavidin
KW - Force spectroscopy
KW - Linker
KW - Unbinding force
UR - http://www.scopus.com/inward/record.url?scp=33751204127&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2006.08.015
DO - 10.1016/j.colsurfb.2006.08.015
M3 - Journal article
C2 - 17023148
AN - SCOPUS:33751204127
VL - 53
SP - 149
EP - 156
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
SN - 0927-7765
IS - 2
ER -
ID: 230977744