Premium
Internal and Global Protein Motion Assessed with a Fusion Construct and In‐Cell NMR Spectroscopy
Author(s) -
Barnes Christopher O.,
Monteith William B.,
Pielak Gary J.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000610
Subject(s) - nuclear magnetic resonance spectroscopy , spectroscopy , construct (python library) , motion (physics) , chemistry , biophysics , biological system , nuclear magnetic resonance , computational biology , analytical chemistry (journal) , physics , biology , stereochemistry , chromatography , computer science , classical mechanics , quantum mechanics , programming language
Motion study: We have examined a fusion protein comprising a globular (ubiquitin) and an intrinsically disordered (α‐synuclein) component. The data show that internal motion determines the quality of in‐cell NMR spectra. The disordered component exhibits a high‐resolution spectrum, whereas the globular portion is only observed when the cells are lysed and diluted.