Structure, Dynamics, and Kinetics of Weak Protein–Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions | Zendy

Salmon Loïc | Zendy; Ortega Roldan JoséLuis | Zendy; Lescop Ewen | Zendy; Licinio Antoine | Zendy; van Nuland Nico | Zendy; Jensen Malene Ringkjøbing | Zendy; Blackledge Martin | Zendy

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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).

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