Title
Co‐translational folding of α‐helical proteins: structural studies of intermediate‐length variants of the λ repressor
Author
Yuya Hanazono, Kazuki Takeda, Kunio Mik
Year
2018
Journal
FEBS Open Bio
Abstract
Nascent polypeptide chains fold co‐translationally 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 co‐translational 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.
Instrument
J-805
Keywords
Circular dichroism, Secondary structure, Chemical stability, Thermal stability, Thermodynamics, Biochemistry