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- W2807988465 abstract "Nascent polypeptide chains fold cotranslationally, but the atomic‐level details of this process remain unknown. Here, we report crystallographic, de novo modeling, and spectroscopic studies of intermediate‐length variants of the λ repressor N‐terminal domain. Although the ranges of helical regions of the half‐length variant were almost identical to those of the full‐length protein, the relative orientations of these helices in the intermediate‐length variants differed. Our results suggest that cotranslational folding of the λ repressor initially forms a helical structure with a transient conformation, as in the case of a molten globule state. This conformation subsequently matures during the course of protein synthesis. Database Structural data are available in the PDB under the accession numbers 5ZCA and 3WOA ." @default.
- W2807988465 created "2018-06-21" @default.
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- W2807988465 date "2018-06-27" @default.
- W2807988465 modified "2023-10-14" @default.
- W2807988465 title "Co‐translational folding of α‐helical proteins: structural studies of intermediate‐length variants of the λ repressor" @default.
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- W2807988465 doi "https://doi.org/10.1002/2211-5463.12480" @default.
- W2807988465 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6070647" @default.
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