Abstract:
:Force spectroscopy is commonly used to measure the kinetics of processes occurring in single biological molecules. These measurements involve attaching the molecule of interest to micron-sized or larger force probes via compliant linkers. Recent theoretical work has described how the properties of the probes and linkers can alter the observed kinetics from the intrinsic behavior of the molecule in isolation. We applied this theory to estimate the errors in measurements of folding made using optical tweezers. Errors in the folding rates arising from instrument artifacts were only ∼20% for constant-force measurements of DNA hairpins with typical choices of linker length and probe size. Measurements of transition paths using a constant trap position at high trap stiffness were also found to be in the low-artifact limit. These results indicate that typical optical trap measurements of kinetics reflect the dynamics of the molecule fairly well, and suggest practical limitations on experimental design to ensure reliable kinetic measurements.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Neupane K,Woodside MTdoi
10.1016/j.bpj.2016.06.011subject
Has Abstractpub_date
2016-07-26 00:00:00pages
283-286issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(16)30449-0journal_volume
111pub_type
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