We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Main Page

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 51: Line 51:
</tr>
</tr>
 +
<tr><td colspan='4' >
 +
<table width='100%' style="padding: 10px; background-color: #d7d8f9; font-size: 2.0em;"><tr>
 +
<td>[[Proteopedia:About|About]]</td>
 +
<td>{{Template:Contact}}</td>
 +
<td>[[Help:Contents|Help]]</td>
 +
</tr></table>
 +
</td></tr>
</table>
</table>

Revision as of 14:29, 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
About this image
Mutations in Coronavirus Spike Protein

by Eric Martz
Black spots are mutations of concern in SARS-CoV-2 spike protein reported by UK scientists in December, 2020. RNA viruses mutate quickly so mutations are expected. These mutations may speed up contagion, but are unlikely to cause more severe COVID-19 and unlikely to reduce vaccine effectiveness. ACE2 binding residues. Animation shows priming via cleavage by furin.
>>> Visit this page >>>

About this image
Molecular Sculpture

by Eric Martz
A historical review on sculptures and physical models of macromolecules.

>>> Visit this page >>>

About this image
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> Visit this I3DC complement >>>

About this image
Transport of Drugs & Nutrients

Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

>>> See more animations and explanation >>>

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

About Image:Contact-email.png Help

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

Personal tools