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<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
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Often it is difficult to utilize the wealth of information found in 3D biomacromolecular structures. Proteopedia's goal is to present structure/function information on these molecules in a user-friendly manner to a broad scientific audience.
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Revision as of 11:17, 21 October 2018

Often it is difficult to utilize the wealth of information found in 3D biomacromolecular structures. Proteopedia's goal is to present structure/function information on these molecules in a user-friendly manner to a broad scientific audience. </td></tr>
ISSN 2310-6301

As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules

Selected Pages Art on Science Journals Education
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Bacteria float with nano-balloons.

ST Huber, D Terwiel, WH Evers, D Maresca, AJ Jakobi. Preprint 2022 doi: 10.1101/2022.05.08.489936
Many kinds of bacteria and archaea control their buoyancy to move to optimal positions in liquid environments. They do this by making nano-compartments called "gas vesicles", long "pipes" with closed ends filled with gases. In 2022, gas vesicle structure was solved, revealing self-assembling thin-walled cylinders of remarkable strength with gas-permeable pores and water-repelling (hydrophobic) interiors. Building on this structural knowledge, gas vesicles are being engineered to serve as biosensors that report via ultrasound.

>>> Visit I3DC Interactive Visualizations >>>

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Molecular Sculpture

by Eric Martz
A historical review on sculptures and physical models of macromolecules.

>>> Visit this page >>>

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Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.

IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

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Introduction to protein structure

This tutorial illustrates some basic properties of protein structure:

  • Levels of protein structure.
  • Ways of representing protein structure.
  • Secondary structures.
  • Motifs in proteins.
  • Domains.
  • Tertiary structure.
  • Quaternary structure.

>>> Visit this page >>>

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