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<b>Proteopedia</b> presents this information in a user-friendly way as a <b>collaborative &amp; free 3D-encyclopedia of proteins &amp; other biomolecules.</b>
<b>Proteopedia</b> presents this information in a user-friendly way as a <b>collaborative &amp; free 3D-encyclopedia of proteins &amp; other biomolecules.</b>
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Revision as of 16:15, 30 September 2025

       ISSN 2310-6301

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

     
       Proteopedia presents this information in a user-friendly way as a collaborative & free 3D-encyclopedia of proteins & other biomolecules.
Selected Research Pages In Journals Education
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HIV-1 protease

by David Canner
The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water.

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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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Make Your Own Electrostatic Potential Maps

Positive (+) and Negative (-) charges on the surface of a protein molecule play crucial roles in its interactions with other molecules, and hence in its functions. Electrostatic potential maps coloring the surface of a protein molecule are a popular way to visualize the distribution of surface charges. Easy to use free software is available to to create these surface maps. Above is an integral membrane potassium channel protein. One of its 4 identical chains is removed so you can see the Negative (-) protein surface contacting the 3 K+ ions.

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