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NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near‐Physiological Conditions
Author(s) -
Gil Sergio,
Hošek Tomáš,
Solyom Zsofia,
Kümmerle Rainer,
Brutscher Bernhard,
Pierattelli Roberta,
Felli Isabella C.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201304272
Subject(s) - amide , intrinsically disordered proteins , solvent , chemistry , proton , proton nmr , characterization (materials science) , nuclear magnetic resonance spectroscopy , chemical physics , materials science , nuclear magnetic resonance , nanotechnology , stereochemistry , organic chemistry , physics , biochemistry , quantum mechanics
When approaching physiological conditions , solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment design. 13 C NMR experiments recover information that is not accessible through amide proton detection, and solvent exchange can be used to increase sensitivity.