Premium
Inside Back Cover: Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins (Angew. Chem. Int. Ed. 45/2017)
Author(s) -
Salvi Nicola,
Abyzov Anton,
Blackledge Martin
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201710486
Subject(s) - cover (algebra) , molecular dynamics , intrinsically disordered proteins , relaxation (psychology) , energy landscape , dynamics (music) , chemical physics , nuclear magnetic resonance spectroscopy , chemistry , materials science , nanotechnology , physics , biophysics , nuclear magnetic resonance , computational chemistry , biology , biochemistry , engineering , mechanical engineering , neuroscience , acoustics
The potential energy landscapes of intrinsically disordered proteins are remarkably flat compared their folded counterparts, making their functional modes difficult to study. In their Communication on page 14020, M. Blackledge and co‐workers use a combination of high‐resolution NMR spectroscopy and advanced molecular dynamics simulation to investigate the extent of functionally important correlated motions in this essential class of proteins.