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Related Concept Videos

Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
Microtubules01:35

Microtubules

There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.
Microtubules01:18

Microtubules

Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer. These αβ-heterodimers...
Microtubule Formation01:23

Microtubule Formation

Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation of...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...

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Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy
07:20

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Published on: February 18, 2022

MTBindingSim: simulate protein binding to microtubules.

Julia T Philip1, Charles H Pence, Holly V Goodson

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. jphilip@nd.edu

Bioinformatics (Oxford, England)
|December 16, 2011
PubMed
Summary

MTBindingSim is a new software tool that helps researchers understand complex protein-protein interactions beyond simple 1:1 binding models. It aids in designing experiments to differentiate various binding scenarios for proteins and polymers.

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Last Updated: May 26, 2026

Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy
07:20

Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy

Published on: February 18, 2022

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: July 20, 2022

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biology

Background:

  • Many protein-protein interactions exhibit complex binding behaviors not explained by simple 1:1 models.
  • Existing tools are limited for recognizing and predicting these complex systems.
  • This complexity hinders the design of experiments to distinguish between different binding models.

Purpose of the Study:

  • To introduce MTBindingSim, a novel software environment for simulating and comparing protein binding models.
  • To provide researchers with a tool to analyze complex protein-protein interactions.
  • To aid in the design of experiments for elucidating binding mechanisms.

Main Methods:

  • MTBindingSim is implemented in MATLAB, allowing execution within MATLAB or as a standalone binary.
  • The software supports Windows, macOS, and Linux operating systems.
  • Source code and binaries are freely available under the GNU General Public License.

Main Results:

  • MTBindingSim enables rapid comparison of various binding models for a given scenario.
  • The simulation environment is particularly tailored for microtubule polymers but applicable to other polymers and protein interactions.
  • Facilitates improved intuition and experimental design for complex binding systems.

Conclusions:

  • MTBindingSim addresses the need for better tools to study complex protein-protein interactions.
  • The software assists researchers in understanding and differentiating intricate binding behaviors.
  • It serves as a valuable resource for both training and experimental planning in molecular and cellular biology.