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<p>[[:Category:Featured in Selected Pages|Other Selected Pages]]</p>
<p>[[:Category:Featured in Selected Pages|Other Selected Pages]]</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to author pages and contribute to Proteopedia]]</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
<p>[[Who knows]] ...</p>
<p>[[Who knows]] ...</p>

Revision as of 07:08, 21 October 2018

ISSN 2310-6301

Because life has more than 2D, Proteopedia helps to understand relationships between structure and function. Proteopedia is a free, collaborative 3D-encyclopedia of proteins & other molecules.


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.

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Opening a Gate to Human Health

by Alice Clark (PDBe)
In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. One of these molecules, ivermectin, is shown in this artwork bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism.

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About this image
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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Tutorial: How do we get the oxygen we breathe

J Prilusky, E Hodis doi: 10.14576/431679.1869588
This tutorial is designed for high school and beginning college students. When we breathe oxygen from the air is taken up by blood in our lungs and soon delivered to each of the cells in our body through our circulatory system. Among other uses, our cells use oxygen as the final electron acceptor in a process called aerobic respiration – a process that converts the energy in food and nutrients into a form of energy that the cell can readily use (molecules of ATP, adenosine triphosphate).

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Other Selected Pages

How to add content to Proteopedia

Video Guides

Who knows ...

Featured in Art

All Art on Science

Featured in I3DC

How to get an Interactive 3D Complement for your paper

List of Interactive Complements

About Interactive 3D Complements

Featured in Education

Teaching Strategies Using Proteopedia

Examples of Pages for Teaching

How to author pages and contribute to Proteopedia

About Image:Contact-email.png Table of Contents Structure Index Help

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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