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Structure, Dynamics, and Kinetics of Weak Protein–Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions
Author(s) -
Salmon Loïc,
Ortega Roldan JoséLuis,
Lescop Ewen,
Licinio Antoine,
van Nuland Nico,
Jensen Malene Ringkjøbing,
Blackledge Martin
Publication year - 2011
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.201100310
Subject(s) - protein dynamics , kinetics , relaxation (psychology) , chemistry , diffusion , chemical physics , dynamics (music) , spin (aerodynamics) , nuclear magnetic resonance , computational chemistry , molecular dynamics , thermodynamics , physics , acoustics , psychology , social psychology , quantum mechanics
Making the invisible visible : Weak protein–protein interactions play a key role in a range of essential biological processes. However, transient or ultraweak complexes cannot be studied in detail by many biophysical techniques. A method based on the measurement of 15 N relaxation rates can be used to study weak protein complexes (see picture; D zz =diffusion tensor).