Protein damage susceptibility (6 Å)

Protein damage susceptibility (7 Å)

Enzymes      Organisms


Fichtner M, Schuster S & Stark H (2020) Determination of scoring functions for protein damage susceptibility. Biosystems 187: 104035. DOI:10.1016/J.BIOSYSTEMS.2019.104035
Fichtner M, Schuster S & Stark H (2019) Data for: Determination of scoring functions for protein damage susceptibility. Mendeley Data, Licence: CC BY 4.0. DOI:10.17632/b2cbxsnvcx.1
Fichtner M, Schuster S & Stark H (2021) Influence of spatial structure on protein damage susceptibility: a bioinformatics approach. Sci Rep 11, 4938. DOI:10.1038/s41598-021-84061-8
Fichtner M, Schuster S & Stark H (2021) Data for: Influence of spatial structure on protein damage susceptibility—A bioinformatics approach. Mendeley Data, Licence: CC BY 4.0. DOI:10.17632/jkmbpfgp4k.1


Low values = less susceptible / High values = more susceptible
Black line = randomly assembled protein (value = 5)
Distribution of all peptides/proteins
Distribution of selected peptides/proteins
Distribution of hidden values
(red)
(blue)
(shortened blue bars)


 
Neuro
 
All
Core
Surface
Only sidechain (-backbone)
Only backbone (-sidechain)
Amyloid
Tau
Prion
Transthyretin


 
Connective tissue
 
All
Core
Surface
Only sidechain (-backbone)
Only backbone (-sidechain)
Collagen
Keratin


 
Toplist (lower)
 
All
Core
Surface
Only sidechain (-backbone)
Only backbone (-sidechain)
Capsid
Flagellin
Spidroin
Antifreeze
Heat shock
Fucose-binding lectin


 
Toplist (higher)
 
All
Core
Surface
Only sidechain (-backbone)
Only backbone (-sidechain)
Toxi
Phospholipase
Phosphatase
Calmodulin


 
Add-On
 
All
Core
Surface
Only sidechain (-backbone)
Only backbone (-sidechain)
Polymerase
DNA
RNA
Ribosomal
NADH
Cytochrome A
Cytochrome B
Cytochrome C
Mitochondral