[NMR paper] Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations
Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations
Proteins are inherently dynamic and their internal motions are essential for biological function. Protein motions cover a broad range of timescales: 10^(-14)-10 s, spanning from sub-picosecond vibrational motions of atoms via microsecond loop conformational rearrangements to millisecond large amplitude domain reorientations. Observing protein dynamics over all timescales and connecting motions and structure to biological mechanisms requires integration of multiple experimental and...
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[NMR paper] Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches
Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches
Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDR) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core and their conformational behavior is strongly influenced by electrostatic interactions. IDPs and IDRs are highly dynamic and a characterization of the motions of IDPs and IDRs is essential for their physically correct description. Nuclear magnetic resonance (NMR) together with molecular...
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Computational approaches to the interpretation of NMR data for studying protein dynamics
Computational approaches to the interpretation of NMR data for studying protein dynamics
2 March 2012
Publication year: 2012
Source:Chemical Physics, Volume 396</br>
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Experimental studies of protein structure and dynamics with NMR provide the classical example of the power of theoretical approaches for the interpretation of experimental results. In this paper we review recent developments in experimental techniques extending the applicability of NMR to the study of protein structure and motion, and advances in the theoretical description.
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An introduction to NMR-based approaches for measuring protein dynamics.
An introduction to NMR-based approaches for measuring protein dynamics.
An introduction to NMR-based approaches for measuring protein dynamics.
Biochim Biophys Acta. 2010 Nov 5;
Authors: Kleckner IR, Foster MP
Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the...