Main Page

ISSN 2310-6301 As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules 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.
Selected Pages	Art on Science	Journals	Education
BREAKTHROUGH in protein structure prediction! by Eric Martz After decades of slow progress by many groups, in 2020, AlphaFold2 proved able to accurately predict the detailed structures of two-thirds of single protein domains from their amino acid sequences. Pictured is AlphaFold2's prediction for the ORF8 protein of SARS-CoV-2 (black), compared with a subsequently published X-ray crystallographic structure (colors). ORF8 contributes to virulence in COVID-19. >>> Visit this page >>>	Molecular Sculpture by Eric Martz A historical review on sculptures and physical models of macromolecules. >>> Visit this page >>>	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 >>>	Tutorial: The Ramachandran principle, phi (φ) and psi (ψ) angles in proteins by Eric Martz The Ramachandran Principle says that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt, because most other conformations are impossible due to steric collisions between atoms. Check Show Clashes to see where non-bonded atoms are overlapping, and thus in physically impossible positions. >>> Visit this tutorial >>>
How to add content to Proteopedia Video Guides Who knows ...	List of Art on Science pages	About Interactive 3D Complements - I3DCs List of I3DCs How to get an I3DC for your paper	Teaching strategies using Proteopedia Examples of pages for teaching How to add content to Proteopedia
About Contact Table of Contents Structure Index Help

Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky, Joel L. Sussman, Angel Herraez