Literature DB >> 29716042

Electro-optic deflectors deliver advantages over acousto-optical deflectors in a high resolution, ultra-fast force-clamp optical trap.

Michael S Woody, Marco Capitanio, E Michael Ostap, Yale E Goldman.   

Abstract

We characterized experimental artifacts arising from the non-linear response of acousto-optical deflectors (AODs) in an ultra-fast force-clamp optical trap and have shown that using electro-optical deflectors (EODs) instead eliminates these artifacts. We give an example of the effects of these artifacts in our ultra-fast force clamp studies of the interaction of myosin with actin filaments. The experimental setup, based on the concept of Capitanio et al. [Nat. Methods 9, 1013-1019 (2012)] utilizes a bead-actin-bead dumbbell held in two force-clamped optical traps which apply a load to the dumbbell to move it at a constant velocity. When myosin binds to actin, the filament motion stops quickly as the total force from the optical traps is transferred to the actomyosin attachment. We found that in our setup, AODs were unsuitable for beam steering due to non-linear variations in beam intensity and deflection angle as a function of driving frequency, likely caused by low-amplitude standing acoustic waves in the deflectors. These aberrations caused instability in the force feedback loops leading to artifactual jumps in the trap position. We demonstrate that beam steering with EODs improves the performance of our instrument. Combining the superior beam-steering capability of the EODs, force acquisition via back-focal-plane interferometry, and dual high-speed FPGA-based feedback loops, we apply precise and constant loads to study the dynamics of interactions between actin and myosin. The same concept applies to studies of other biomolecular interactions.

Entities:  

Year:  2018        PMID: 29716042      PMCID: PMC6005679          DOI: 10.1364/OE.26.011181

Source DB:  PubMed          Journal:  Opt Express        ISSN: 1094-4087            Impact factor:   3.894


  20 in total

1.  Single kinesin molecules studied with a molecular force clamp.

Authors:  K Visscher; M J Schnitzer; S M Block
Journal:  Nature       Date:  1999-07-08       Impact factor: 49.962

2.  An automated two-dimensional optical force clamp for single molecule studies.

Authors:  Matthew J Lang; Charles L Asbury; Joshua W Shaevitz; Steven M Block
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

3.  The motor protein myosin-I produces its working stroke in two steps.

Authors:  C Veigel; L M Coluccio; J D Jontes; J C Sparrow; R A Milligan; J E Molloy
Journal:  Nature       Date:  1999-04-08       Impact factor: 49.962

4.  Force generation in single conventional actomyosin complexes under high dynamic load.

Authors:  Yasuharu Takagi; Earl E Homsher; Yale E Goldman; Henry Shuman
Journal:  Biophys J       Date:  2005-12-02       Impact factor: 4.033

5.  Interference model for back-focal-plane displacement detection in optical tweezers.

Authors:  F Gittes; C F Schmidt
Journal:  Opt Lett       Date:  1998-01-01       Impact factor: 3.776

6.  Unbinding force of a single motor molecule of muscle measured using optical tweezers.

Authors:  T Nishizaka; H Miyata; H Yoshikawa; S Ishiwata; K Kinosita
Journal:  Nature       Date:  1995-09-21       Impact factor: 49.962

7.  Bead movement by single kinesin molecules studied with optical tweezers.

Authors:  S M Block; L S Goldstein; B J Schnapp
Journal:  Nature       Date:  1990-11-22       Impact factor: 49.962

8.  Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap.

Authors:  W H Guilford; D E Dupuis; G Kennedy; J Wu; J B Patlak; D M Warshaw
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

9.  Implementation and Tuning of an Optical Tweezers Force-Clamp Feedback System.

Authors:  Michael Bugiel; Anita Jannasch; Erik Schäffer
Journal:  Methods Mol Biol       Date:  2017

10.  Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke.

Authors:  Marco Capitanio; Monica Canepari; Manuela Maffei; Diego Beneventi; Carina Monico; Francesco Vanzi; Roberto Bottinelli; Francesco Saverio Pavone
Journal:  Nat Methods       Date:  2012-09-02       Impact factor: 28.547

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  5 in total

1.  The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.

Authors:  Brandon M Bensel; Michael S Woody; Serapion Pyrpassopoulos; Yale E Goldman; Susan P Gilbert; E Michael Ostap
Journal:  Proc Natl Acad Sci U S A       Date:  2020-06-22       Impact factor: 11.205

Review 2.  Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?

Authors:  Alf Månsson; Marko Ušaj; Luisa Moretto; Dilson E Rassier
Journal:  Int J Mol Sci       Date:  2018-06-25       Impact factor: 5.923

3.  Single molecule mechanics resolves the earliest events in force generation by cardiac myosin.

Authors:  Michael S Woody; Donald A Winkelmann; Marco Capitanio; E Michael Ostap; Yale E Goldman
Journal:  Elife       Date:  2019-09-17       Impact factor: 8.140

4.  Myosin with hypertrophic cardiac mutation R712L has a decreased working stroke which is rescued by omecamtiv mecarbil.

Authors:  Aaron Snoberger; Bipasha Barua; Jennifer L Atherton; Henry Shuman; Eva Forgacs; Yale E Goldman; Donald A Winkelmann; E Michael Ostap
Journal:  Elife       Date:  2021-02-19       Impact factor: 8.140

5.  Positive cardiac inotrope omecamtiv mecarbil activates muscle despite suppressing the myosin working stroke.

Authors:  Michael S Woody; Michael J Greenberg; Bipasha Barua; Donald A Winkelmann; Yale E Goldman; E Michael Ostap
Journal:  Nat Commun       Date:  2018-09-21       Impact factor: 14.919

  5 in total

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