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Related Concept Videos

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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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.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Unsymmetrical bending occurs when a structural member is subjected to bending moments in a plane that does not align with the member's principal axes. This scenario typically arises in beams and other structural components when loads are applied at non-ideal angles, introducing complexities in stress analysis.
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In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
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Finite Element Modelling of a Cellular Electric Microenvironment
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CCBuilder 2.0: Powerful and accessible coiled-coil modeling.

Christopher W Wood1, Derek N Woolfson1,2,3

  • 1School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, United Kingdom.

Protein Science : a Publication of the Protein Society
|August 25, 2017
PubMed
Summary
This summary is machine-generated.

CCBuilder 2.0 simplifies biomolecular engineering by modeling alpha-helical coiled coils and collagen triple helices. This web application aids protein structure determination and the design of novel protein assemblies.

Keywords:
coiled coilcollagencomputational designparametric designprotein designstructural bioinformaticsstructural modelingsynthetic biologyweb app

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Area of Science:

  • Biomolecular modeling and engineering
  • Structural bioinformatics
  • Computational biology

Background:

  • Accessible computational tools are crucial for advancing biomolecular engineering and design.
  • Parametric modeling of complex 3D protein folds, such as alpha-helical coiled coils (3-5% of known proteins), remains a challenge.
  • Alpha-helical coiled coils are protein structures composed of bundled alpha helices, describable by a limited set of parameters.

Purpose of the Study:

  • To develop an easy-to-use web application, CCBuilder 2.0, for modeling and optimizing protein structures.
  • To enable the parametric description and modeling of alpha-helical coiled coils and polyproline-based collagen triple helices.
  • To expand the application of biomolecular engineering through accessible computational tools.

Main Methods:

  • Development of CCBuilder 2.0, a web-based application for protein structure modeling.
  • Implementation of parametric equations to represent the 3D structures of alpha-helical coiled coils.
  • Making the CCBuilder 2.0 application freely available as open-source software.

Main Results:

  • CCBuilder 2.0 provides a user-friendly platform for modeling alpha-helical coiled coils and collagen triple helices.
  • The application facilitates in silico model building, protein assembly design, and the creation of de novo protein structures.
  • CCBuilder 2.0 aids in molecular replacement for X-ray crystallography and the engineering of novel protein designs.

Conclusions:

  • CCBuilder 2.0 enhances the accessibility of biomolecular modeling for a significant class of proteins.
  • The tool supports diverse applications, from fundamental protein structure determination to advanced protein engineering and biotechnology.
  • The open-source nature of CCBuilder 2.0 promotes wider adoption and contribution within the scientific community.