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The local topological free energy of proteins

Quenisha Baldwin, Eleni Panagiotou
doi: https://doi.org/10.1101/2021.01.06.425494
Quenisha Baldwin
#Department of Biology, Tuskegee University, AL 36088, USA <>
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  • For correspondence: qbaldwin8382@tuskegee.edu qbaldwin8382@tuskegee.edu
Eleni Panagiotou
§Department of Mathematics and SimCenter, University of Tennessee at Chattanooga, TN 37403, USA <>
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  • For correspondence: eleni-panagiotou@utc.edu
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Abstract

Protein folding, the process by which proteins attain a 3-dimensional conformation necessary for their function, remains an important unsolved problem in biology. A major gap in our understanding is how local properties of proteins relate to their global properties. In this manuscript, we use the Writhe and Torsion to introduce a new local topological/geometrical free energy that can be associated to 4 consecutive residues along protein backbone. By analyzing a culled protein dataset from the PDB, our results show that high local topological free energy conformations are independent of sequence and may be involved in the rate limiting step in protein folding. By analyzing a set of 2-state single domain proteins, we find that the total local topological free energy of these proteins correlates with the experimentally observed folding rates reported in [29].

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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Posted January 08, 2021.
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The local topological free energy of proteins
Quenisha Baldwin, Eleni Panagiotou
bioRxiv 2021.01.06.425494; doi: https://doi.org/10.1101/2021.01.06.425494
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The local topological free energy of proteins
Quenisha Baldwin, Eleni Panagiotou
bioRxiv 2021.01.06.425494; doi: https://doi.org/10.1101/2021.01.06.425494

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