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.

Journal:Proteins:3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 22: Line 22:
|-
|-
|<applet load='1856 RTF Morph backbone.pdb' name='RTF' size='300' frame='true' scene='96/964832/1856_rtf_morph_backbone/1'/>
|<applet load='1856 RTF Morph backbone.pdb' name='RTF' size='300' frame='true' scene='96/964832/1856_rtf_morph_backbone/1'/>
-
|[[Image:1856 ESM.jpgsize='300']]
+
|[[Image:1856 ESM.jpg size='300']]
|<applet load='1856 AF2 Morph backbone.pdb"' name='AF2' size='300' frame='true' scene='96/964832/1856_af_morph_backbone/2'/>
|<applet load='1856 AF2 Morph backbone.pdb"' name='AF2' size='300' frame='true' scene='96/964832/1856_af_morph_backbone/2'/>
|}
|}

Revision as of 10:40, 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].


RTF-1856 ESM-1856 AF2-1856
Drag the structure with the mouse to rotate
Image:1856 ESM.jpg size='300'
Drag the structure with the mouse to rotate



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


sample

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.
Personal tools