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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.
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How to add content to Proteopedia Video Guides Who knows ... Green Fluorescent Protein by Eran Hodis Green fluorescent protein (GFP) is a bioluminescent polypeptide isolated from the jellyfish Aequorea victoria. GFP converts the blue chemiluminescence of aequorin into green fluorescent light. In the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, or interactions between various membrane and cytoplasmic proteins. >>> Visit this page >>>	About Interactive 3D Complements - I3DCs List of I3DCs How to get an I3DC for your paper 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. >>> Visit this I3DC complement >>>	Teaching strategies using Proteopedia Examples of pages for teaching How to add content to Proteopedia Touch-Sensitive Channel Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions. >>> See more animations and explanation >>>
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