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Related Concept Videos

ATP Driven Pumps I: An Overview01:27

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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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ATP Synthase: Mechanism01:48

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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ATP Driven Pumps III: V-type Pumps01:30

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V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
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ATP Driven Pumps II: P-type Pumps01:34

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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
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ATP Synthase: Structure01:18

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
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Related Experiment Video

Updated: Jan 7, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

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External torque application to molecular motor F1-ATPase using optical vortex trapping.

Yu Hashimoto1, Tomoko Otsu-Hyodo1, Yu Takiguchi1

  • 1Hamamatsu Photonics K.K., Central Research Laboratory, Hamamatsu, Shizuoka, Japan.

Biophysical Journal
|January 2, 2026
PubMed
Summary
This summary is machine-generated.

Researchers developed a new optical tweezers method using optical vortices (OVs) to precisely control molecular motors. This technique enables quantitative mechanical manipulation and torque measurement for biomolecules like F1-ATPase.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Optical Physics

Background:

  • Single-molecule manipulation is crucial for understanding biological mechanisms.
  • Optical tweezers are widely used but struggle with applying constant torque for rotational motion.
  • Measuring torque on moving molecules presents significant challenges.

Purpose of the Study:

  • To develop a method for quantitative mechanical manipulation of biomolecules using optical tweezers.
  • To enable precise application of constant torque to molecular motors.
  • To measure the torque generated by molecular motors.

Main Methods:

  • Adaptation of optical tweezers to generate optical vortices (OVs) via phase modulation.
  • Utilizing a DNA origami rod as a precise handle for torque application.
  • Applying controlled torque to the molecular motor F1-ATPase using OV-equipped optical tweezers.

Main Results:

  • Optical vortices enabled quantitative mechanical manipulations with optical tweezers.
  • The developed technique allowed for the measurement of torque generated by a molecular motor.
  • Constant torque application via OVs successfully stalled and reversed the rotation of F1-ATPase.

Conclusions:

  • Optical vortices offer a novel approach for precise torque application in single-molecule studies.
  • This technique advances the ability to quantitatively investigate molecular motor function.
  • The method is valuable for applying constant torque to various biomolecules.