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Charge‐Induced Molecular Alignment of Intrinsically Disordered Proteins
Author(s) -
Skora Lukasz,
Cho MinKyu,
Kim HaiYoung,
Becker Stefan,
Fernandez Claudio O.,
Blackledge Martin,
Zweckstetter Markus
Publication year - 2006
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.200602317
Subject(s) - intrinsically disordered proteins , biomolecule , chemical physics , charge (physics) , dipole , electrostatics , molecular dynamics , conformational ensembles , ionic strength , chemistry , ionic bonding , nanotechnology , materials science , computer science , physics , computational chemistry , nuclear magnetic resonance , ion , quantum mechanics , organic chemistry , aqueous solution
NMR dipolar couplings are a sensitive spectroscopic probe of the structure and dynamics of biomolecules. It is demonstrated that molecular alignment of intrinsically disordered proteins depends critically on electrostatic interactions, is scaled with the ionic strength of the solution, and can be predicted by using a simplified electrostatic model.