Folding on the assembly line.
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.
Haas
Elisha
E
The Mina Everard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat-Gan, Israel. haas@mail.biu.ac.il
D001059:Apoproteins / Q000096:biosynthesis* / Q000737:chemistry; D001896:Boron Compounds / Q000737:chemistry; D005454:Fluorescence Polarization; D009211:Myoglobin / Q000096:biosynthesis* / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D012270:Ribosomes / Q000378:metabolism / Q000648:ultrastructure*
C095489:4,4-difluoro-4-bora-3a,4a-diaza-s-indacene; D001059:Apoproteins; D001896:Boron Compounds; D009211:Myoglobin; C010857:apomyoglobin