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Bacterial flagellins: does only size matter?

Shchyogolev, S. Y.; Burygin, G. L.; Matora, L. Y.

2020-06-15 molecular biology
10.1101/2020.06.15.151936 bioRxiv
Show abstract

The protein sequences of a number of Azospirillaceae strains were investigated that contain the pf00669 domain and belong to a variety of bacterial flagellum systems with unusually large flagellin sizes. A set of tools for the homologous and template-based modeling of protein structures was used to reveal the probability of alternative folding, i.e., generation of two protein models with significantly different 3D structures and functions (flagellin or S-layer protein) for a single amino acid sequence.

Matching journals

The top 8 journals account for 50% of the predicted probability mass.

1
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Top 12%
15.1%
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2
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3.3%
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Top 0.7%
3.2%
50% of probability mass above
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Top 2%
2.1%
10
Computational and Structural Biotechnology Journal
● 242 papers in training set
Top 3%
2.1%
11
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Top 0.1%
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2.0%
13
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Top 5%
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Top 0.6%
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15
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Top 0.1%
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Top 1%
1.5%
17
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1.3%
18
Current Microbiology
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Top 0.5%
1.1%
19
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○ 36 papers in training set
Top 0.2%
1.1%
20
Pharmaceuticals
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Top 0.9%
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1.0%
22
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◐ 61 papers in training set
Top 2%
0.8%
24
Heliyon
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Top 8%
0.8%
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0.8%
26
PROTEOMICS
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Top 0.7%
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"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.