PT  - JOURNAL ARTICLE
AU  - Meghan W. Franklin
AU  - Joanna Krise
AU  - Jacqueline J. Stevens
AU  - Joanna S.G. Slusky
TI  - Redesigning OmpA Loops Using Canonical Outer Membrane Protein Loop Structures
AID  - 10.1101/2020.10.08.331546
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.10.08.331546
4099  - http://biorxiv.org/content/early/2020/10/08/2020.10.08.331546.short
4100  - http://biorxiv.org/content/early/2020/10/08/2020.10.08.331546.full
AB  - Protein loops can be difficult to design and predict. There have been multiple different algorithms developed to predict the structure of loops. Outer membrane proteins are all beta barrels and these barrels have a variety of well-documented loop conformations. Here we test three different algorithms to predict the structure of outer membrane protein loops. We find the PETALS algorithm is superior for this purpose. We then experimentally test the effect of replacing the long loops of outer membrane protein OmpA with twelve shorter designed loops. Though we succeeded in creating the smallest known outer membrane barrel, we find that the designed loops do not have a strong effect on OmpA folding.Competing Interest StatementThe authors have declared no competing interest.