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Tlusty, Tsvi
Living and Soft Matter Theory Group
Research Interests
  • Systems biology, non-equilibrium physics, physical biology, molecular information, proteins

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Slowest-first protein translation scheme: Structural asymmetry and co-translational folding

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dc.contributor.author McBride, John M. ko
dc.contributor.author Tlusty, Tsvi ko
dc.date.available 2021-12-31T00:10:02Z -
dc.date.created 2021-12-28 ko
dc.date.issued 2021-12 ko
dc.identifier.citation BIOPHYSICAL JOURNAL, v.120, no.24, pp.5466 - 5477 ko
dc.identifier.issn 0006-3495 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/55686 -
dc.description.abstract Proteins are translated from the N to the C terminus, raising the basic question of how this innate directionality affects their evolution. To explore this question, we analyze 16,200 structures from the Protein Data Bank (PDB). We find remarkable enrichment of α helices at the C terminus and β strands at the N terminus. Furthermore, this α−β asymmetry correlates with sequence length and contact order, both determinants of folding rate, hinting at possible links to co-translational folding (CTF). Hence, we propose the “slowest-first” scheme, whereby protein sequences evolved structural asymmetry to accelerate CTF: the slowest of the cooperatively folding segments are positioned near the N terminus so they have more time to fold during translation. A phenomenological model predicts that CTF can be accelerated by asymmetry in folding rate, up to double the rate, when folding time is commensurate with translation time; analysis of the PDB predicts that structural asymmetry is indeed maximal in this regime. This correspondence is greater in prokaryotes, which generally require faster protein production. Altogether, this indicates that accelerating CTF is a substantial evolutionary force whose interplay with stability and functionality is encoded in secondary structure asymmetry. © 2021 Biophysical Society ko
dc.language 영어 ko
dc.publisher CELL PRESS ko
dc.title Slowest-first protein translation scheme: Structural asymmetry and co-translational folding ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-85121215692 ko
dc.identifier.wosid 000734719100006 ko
dc.type.rims ART ko
dc.identifier.doi 10.1016/j.bpj.2021.11.024 ko
dc.identifier.url https://www.sciencedirect.com/science/article/pii/S0006349521009930?via%3Dihub ko
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