Developing limited proteolysis and mass spectrometry for the characterization of ribosome topography

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A comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometry

The kinetics and thermodynamics of protein folding are commonly studied in vitro by denaturing/renaturing intact protein sequences. How these folding mechanisms relate to de novo folding that occurs as the nascent polypeptide emerges from the ribosome is much less well understood. Here, we have employed limited proteolysis followed by mass spectrometry analyses to compare directly free and ribo...

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ژورنال

عنوان ژورنال: Journal of the American Society for Mass Spectrometry

سال: 2007

ISSN: 1044-0305,1879-1123

DOI: 10.1016/j.jasms.2007.03.028