Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Introduction to Actin

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across different species.

Actin Filament Depolymerization

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

Crystal Field Theory - Octahedral Complexes

Crystal Field Theory - Octahedral Complexes

Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Stabilising high-spin, high-valent transition-metal-oxo species in cucurbit[5]uril: correlating structure, spin state, and reactivity.

Physical chemistry chemical physics : PCCP·2026

Same author

Proton-coupled electron transfer modulates the metal release of blood serum iron transferrin.

Dalton transactions (Cambridge, England : 2003)·2025

Same author

Tuning the lanthanide binding tags for preferential actinide chelation: an all atom molecular dynamics study.

Physical chemistry chemical physics : PCCP·2025

Same author

Synthesis, Structure, and Redox Reactivity of Ni Complexes Bearing a Redox and Acid-Base Non-innocent Ligand with Ni<sup>II</sup>, Ni<sup>III</sup>, and Ni<sup>IV</sup> Formal Oxidation States.

Journal of the American Chemical Society·2025

Same author

Fatty acid influence on zinc and uranyl ion binding to human serum albumin: an all atoms molecular dynamics investigation.

Journal of biomolecular structure & dynamics·2024

Same author

Manifold Fluorescence Enhancement of a Styryl(pyridinium)-chromene Hybrid Dye upon Binding with an Elongated β-Cyclodextrin Cavity.

The journal of physical chemistry. B·2024

Search research articles

Related Experiment Video

Updated: May 23, 2026

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Can functionalized cucurbituril bind actinyl cations efficiently? A density functional theory based investigation.

Mahesh Sundararajan¹, Vivek Sinha, Tusar Bandyopadhyay

¹Theoretical Chemistry Section, Bhabha Atomic Research Centre, Mumbai 400 085, India. smahesh@barc.gov.in

The Journal of Physical Chemistry. A

|April 5, 2012

Summary

This summary is machine-generated.

Cucurbituril molecules show potential for binding actinyl cations. Functionalization with methyl or cyclohexyl groups enhances binding, while fluorination reduces it, offering insights into actinyl complexation.

More Related Videos

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Measuring Protein Binding to F-actin by Co-sedimentation

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

Related Experiment Videos

Last Updated: May 23, 2026

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Measuring Protein Binding to F-actin by Co-sedimentation

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

Area of Science:

Computational chemistry
Supramolecular chemistry
Radiochemistry

Background:

Actinyl cations pose significant challenges in nuclear waste management and environmental remediation.
Host-guest chemistry offers potential solutions for sequestering and stabilizing these hazardous ions.
Cucurbiturils are macrocyclic host molecules with tunable properties for molecular recognition.

Purpose of the Study:

To investigate the feasibility of cucurbituril host molecules as actinyl cation binders.
To analyze binding sites and affinities of cucurbiturils towards uranyl and other actinyls.
To evaluate the impact of cucurbituril functionalization on actinyl binding.

Main Methods:

Density functional theory (DFT) calculations were employed to model interactions.
Binding energies, structural parameters, and vibrational spectra were computed.
Various cucurbituril derivatives with different functional groups were analyzed.

Main Results:

The μ(5)-binding mode of cucurbit[5]uril to uranyl was predicted as the most favorable.
Functionalization with methyl and cyclohexyl groups enhanced actinyl binding affinities.
Fluorination decreased actinyl binding affinities compared to the native cucurbituril.
Hydroxylation of cucurbituril did not differentiate between actinyl oxidation states.

Conclusions:

Cucurbiturils are promising candidates for actinyl cation binding, with functionalization offering a route to tune affinity.
Specific functional groups can significantly enhance or diminish binding, providing design principles for selective actinyl sequestration.
DFT calculations are a valuable tool for predicting host-guest interactions in complex systems.