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Structure and dynamics of ribosome‐bound nascent chains: insights from NMR spectroscopy (752.2)
Author(s) -
Christodoulou John
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.752.2
Subject(s) - ribosome , nuclear magnetic resonance spectroscopy , folding (dsp implementation) , chemistry , protein folding , biophysics , translation (biology) , polypeptide chain , two dimensional nuclear magnetic resonance spectroscopy , side chain , crystallography , biochemistry , rna , stereochemistry , biology , messenger rna , amino acid , electrical engineering , gene , engineering , organic chemistry , polymer
The folding processes of nascent chains are intricately linked to their chain elongation, which occurs in a vectorial manner as the N‐terminal part of the nascent chain emerges from the ribosome. Our use of NMR spectroscopy on ribosomes and ribosome nascent‐chain complexes (RNCs) is providing detailed structural insights of the conformations of protein chains while they are being created on the ribosome. By producing in‐vivo derived RNCs in which the nascent polypeptide is selectively labelled, our recent work has allowed us to use NMR follow, at a residue‐specific level, the co‐translational folding processes of proteins of several topologies, specifically, an immunoglobulin‐domain and of the intrinsically disordered protein, alpha‐synuclein. Recent developments in our use of NMR data (including the chemical shift alone) to produce the first experimentally derived structures of ribosome nascent chain folding and also in‐cell NMR studies to probe proteins and nascent chains within their physiological environment will also be discussed.