Protein folding: understanding the role of water and the low Reynolds number environment as the peptide chain emerges from the ribosome and folds

DOI10.1016/J.JTBI.2014.07.025zbMath1309.92062OpenAlexW2034691298WikidataQ87648237 ScholiaQ87648237MaRDI QIDQ2341163

Siddhartha Sen, H. Paul Voorheis

Publication date: 23 April 2015

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/j.jtbi.2014.07.025

zbMATH Keywords

quantum field theoryprotein biosynthesiscoherent domainsrole of hydophobic amino acidswater sheath

Mathematics Subject Classification ID

Biochemistry, molecular biology (92C40) Protein sequences, DNA sequences (92D20)

Uses Software

• MOE

Cites Work

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• Characteristic forms and geometric invariants
• Pattern synthesis from singular solutions in the Debye limit: helical waves and twisted toroidal scroll structures
• Geometry of self-propulsion at low Reynolds number

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