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<p>[[Help:Contents#For_authors:_contributing_content|How to author pages and contribute to Proteopedia]]</p>
<p>[[Help:Contents#For_authors:_contributing_content|How to author pages and contribute to Proteopedia]]</p>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[Who knows]] ...</p>
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Revision as of 14:12, 18 October 2018

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. ISSN 2310-6301

Selected Pages Art on Science Journals Education
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Coronavirus Spike Protein Priming

by Eric Martz
Coronavirus SARS-CoV-2 (responsible for COVID-19) has a spike protein on its surface, which enables it to infect host cells. Initially, proteases in the lungs clip the homo-trimeric spike protein at a unique sequence. This primes it, causing it to extend its receptor binding surface (shown in the above animation), optimizing binding to the host cell's ACE2 receptor (not shown). Next, spike protein initiates fusion of the virus and host cell membranes (not shown), enabling the virus RNA to enter the cell and initiate production of new virions. Knowledge of spike protein's molecular structure and function is crucial to developing effective therapies and vaccines.
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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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Geobacter nanowire structure surprise.

F Wang, Y Gu, JP O'Brien, SM Yi, SE Yalcin, V Srikanth, C Shen, D Vu, NL Ing, AI Hochbaum, EH Egelman, NS Malvankar. Cell 2019 doi: 10.1016/j.cell.2019.03.029
Bacteria living in anaerobic environments (no oxygen) need alternative electron acceptors in order to get energy from their food. An acceptor abundant in the earth's crust is red iron oxide ("rust"), which gets reduced to black iron oxide (magnetite). Many bacteria, such as Geobacter, get their metabolic energy by transferring electrons to acceptors that are multiple cell diameters distant, using protein nanowires. These were long thought to be pili. But when the structure of the nanowires was solved in 2019, to everyone's surprise, they turned out to be unprecedented linear polymers of multi-heme cytochromes. The hemes form an electrically conductive chain in the cores of these nanowires.

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Tutorial: Ramachandran Plot Inspection

by Angel Herráez
Side-by-side display of dihedral angles in a 3D model of a tripeptide and its Ramachandran plot. Users can interact with any of them and the other will change accordingly. Includes animated rotations with display of clashes.

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Other Selected Pages More Art on Science Other Journals More on Education

How to author pages and contribute to Proteopedia

Video Guides

Who knows ...

How to get an Interactive 3D Complement for your paper

List of Interactive Complements

About Interactive 3D Complements

Teaching Strategies Using Proteopedia

Examples of Pages for Teaching

How to author pages and contribute to Proteopedia

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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