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Related Concept Videos

Actin Treadmilling01:18

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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Single Nucleotide Polymorphisms-SNPs01:05

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A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
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Introduction to Actin01:26

Introduction to Actin

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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...
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Actin Polymerization01:42

Actin Polymerization

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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...
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Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism01:21

Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism

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Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Related Experiment Video

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Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
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Structural Polymorphism of Actin.

Toshiro Oda1, Shuichi Takeda2, Akihiro Narita2

  • 1Faculty of Health and Welfare, Tokai Gakuin University, 5-68 Nakakirino-cho, Kakamigahara, Gifu 504-8511, Japan.

Journal of Molecular Biology
|June 11, 2019
PubMed
Summary
This summary is machine-generated.

Researchers identified four actin conformation groups (F, C, O, G) by analyzing over 200 structures. Molecular dynamics revealed that G-form actin structures are convertible, unlike F- and C-forms, aiding functional mechanism understanding.

Keywords:
clusteringconformational spacedomain orientationprotein assemblyrigid bodies

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Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein structural polymorphism is key to understanding atomic-level function.
  • Over 200 atomic structures of actin exist, studied via crystallography, fiber diffraction, and electron microscopy.

Purpose of the Study:

  • To characterize reported actin structures and identify distinct conformational groups.
  • To investigate the convertibility and accessibility between different actin conformations.

Main Methods:

  • Analysis of over 200 published atomic structures of actin.
  • Development of parameters based on discrete rigid bodies within the actin molecule.
  • Cluster analysis to identify conformation groups.
  • Molecular dynamics simulations to evaluate structural convertibility and accessibility.

Main Results:

  • Identification of four distinct actin conformation groups: F-form (naked F-actin), C-form (cofilactin), O-form (profilin-actin), and G-form (most crystal structures).
  • The G-form exhibited the most variations, with conformational changes convertible via thermal fluctuation.
  • F- and C-forms were found to be inaccessible from the G-form.

Conclusions:

  • Actin exhibits distinct conformational states with varying interconversion dynamics.
  • Understanding these conformational conversions is crucial for elucidating actin's functional mechanisms at the atomic level.