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Journal:Proteins:3

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extra stuff:
 
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<scene name='96/964832/Hco_af2_top_model/1'>opening</scene>
 
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&lt; and &gt; signs.
 
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 
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== Function ==
 
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== Disease ==
 
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== Relevance ==
 
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== Structural highlights ==
 
sample <scene name='96/964832/Hco_af2_top_model/3'>rocket/tract</scene>
sample <scene name='96/964832/Hco_af2_top_model/3'>rocket/tract</scene>
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
== References ==
== References ==
<references/>
<references/>

Revision as of 09:11, 4 May 2023

Do Newly Born orphan proteins resemble Never Born proteins? A study using three deep learning algorithms

Newly Born proteins, or orphan proteins, have no sequence homology to other proteins and occur in single species or within a taxonomically restricted gene family

Never Born proteins are random polypeptides with amino acid content similar to that of native proteins.

Can recently developed AI/Deep Learning tools for predicting 3D protein structures like:

  • AlphaFold2 (AF2)
  • RoseTTAFold (RTF)
  • Evolutionary Scale Modeling (ESM-2)

be useful to see if Newly Born proteins are similar to Never Born proteins?

Sequences of Never Born proteins by Tretyachenko et al.[1] showed experimentally that some folded into compact structures [Fig. 1], while others belong to the category of intrinsically disordered proteins (IDPs)[2] [Fig. 2].


Never Born 1856 AF2

Drag the structure with the mouse to rotate









sample


References

  1. Tretyachenko V, Vymětal J, Bednárová L, Kopecký V Jr, Hofbauerová K, Jindrová H, Hubálek M, Souček R, Konvalinka J, Vondrášek J, Hlouchová K. Random protein sequences can form defined secondary structures and are well-tolerated in vivo. Sci Rep. 2017 Nov 13;7(1):15449. PMID:29133927 doi:10.1038/s41598-017-15635-8
  2. Dunker AK, Silman I, Uversky VN, Sussman JL. Function and structure of inherently disordered proteins. Curr Opin Struct Biol. 2008 Dec;18(6):756-64. Epub 2008 Nov 17. PMID:18952168 doi:10.1016/j.sbi.2008.10.002

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
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