Open AccessFolding on the Assembly Line
Author(s) -
Elisha Haas
Publication year - 2008
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb800216n
Subject(s) - elongation , ribosome , biophysics , folding (dsp implementation) , protein folding , polypeptide chain , chemistry , fluorescence anisotropy , crystallography , biology , biochemistry , rna , materials science , amino acid , membrane , ultimate tensile strength , electrical engineering , metallurgy , gene , engineering
Deciphering the mechanism of folding of newly synthesized proteins in the cell is a major challenge because of the large size and multiplicity of molecular components involved and the asynchrony of biosynthesis. Fluorescently labeled ribosome-bound nascent chains of a defined length were prepared and subjected to dynamic fluorescence depolarization spectroscopy measurements. Nanosecond anisotropy decay correlation times of proteins' nascent chains at different stages of polypeptide elongation were determined for the first time. Striking dependence of the chain dynamics on the stages of elongation was observed and revealed chain length dependence of folding on the ribosome.