[NMR paper] Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Related ArticlesAnalysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Abstract
We report a new multidimensional magic angle spinning NMR methodology, which provides an accurate and detailed probe of molecular motions occurring on timescales of nano- to microseconds, in sidechains of proteins. The approach is based on a 3D CPVC-RFDR correlation experiment recorded under fast MAS conditions (?R = 62 kHz), where (13)C-(1)H CPVC dipolar lineshapes are recorded in a chemical shift resolved manner. The power of the technique is demonstrated in model tripeptide Tyr-(d)Ala-Phe and two nanocrystalline proteins, GB1 and LC8. We demonstrate that, through numerical simulations of dipolar lineshapes of aromatic sidechains, their detailed dynamic profile, i.e., the motional modes, is obtained. In GB1 and LC8 the results unequivocally indicate that a number of aromatic residues are dynamic, and using quantum mechanical calculations, we correlate the molecular motions of aromatic groups to their local environment in the crystal lattice. The approach presented here is general and can be readily extended to other biological systems.
PMID: 26451400 [PubMed - as supplied by publisher]
[NMR paper] Local Isotropic Diffusion Approximation for Coupled Internal and Overall Molecular Motions in NMR Spin Relaxation.
Local Isotropic Diffusion Approximation for Coupled Internal and Overall Molecular Motions in NMR Spin Relaxation.
Related Articles Local Isotropic Diffusion Approximation for Coupled Internal and Overall Molecular Motions in NMR Spin Relaxation.
J Phys Chem B. 2014 Aug 28;
Authors: Gill ML, Palmer AG
Abstract
The present work demonstrates that NMR spin relaxation rate constants for molecules interconverting between states with different diffusion tensors can be modeled theoretically by combining orientational correlation...
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[NMR paper] Quantitative Quantum Mechanical Spectral Analysis (qQMSA) of (1)H NMR spectra of complex mixtures and biofluids.
Quantitative Quantum Mechanical Spectral Analysis (qQMSA) of (1)H NMR spectra of complex mixtures and biofluids.
Related Articles Quantitative Quantum Mechanical Spectral Analysis (qQMSA) of (1)H NMR spectra of complex mixtures and biofluids.
J Magn Reson. 2014 Feb 18;242C:67-78
Authors: Tiainen M, Soininen P, Laatikainen R
Abstract
The quantitative interpretation of (1)H NMR spectra of mixtures like the biofluids is a demanding task due to spectral complexity and overlap. Complications may arise also from water suppression, T2-editing,...
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[NMR paper] Quantitative Quantum Mechanical Spectral Analysis (qQMSA) of 1H NMR Spectra of Complex Mixtures and Biofluids
Quantitative Quantum Mechanical Spectral Analysis (qQMSA) of 1H NMR Spectra of Complex Mixtures and Biofluids
Publication date: Available online 18 February 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Mika Tiainen , Pasi Soininen , Reino Laatikainen</br>
The quantitative interpretation of 1H NMR spectra of mixtures like the biofluids is a demanding task due to spectral complexity and overlap. Complications may arise also from water suppression, T2-editing, protein interactions, relaxation differences of the species, experimental artifacts and,...
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[NMR paper] NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
J Phys Chem B. 2013 May 2;
Authors: Xia J, Deng NJ, Levy RM
Abstract
Calculating NMR relaxation effects for proteins with dynamics on multiple timescales generally requires very long trajectories based on conventional molecular dynamics simulations. In this report,...
[NMR paper] NMR structure determination of proteins supplemented by quantum chemical calculations
NMR structure determination of proteins supplemented by quantum chemical calculations: detailed structure of the Ca2+ sites in the EGF34 fragment of protein S.
Related Articles NMR structure determination of proteins supplemented by quantum chemical calculations: detailed structure of the Ca2+ sites in the EGF34 fragment of protein S.
J Biomol NMR. 2005 Feb;31(2):97-114
Authors: Hsiao YW, Drakenberg T, Ryde U
We present and test two methods to use quantum chemical calculations to improve standard protein structure refinement by molecular...
[Question from NMRWiki Q&A forum] NMR experiments to assign aromatic sidechains?
NMR experiments to assign aromatic sidechains?
Hello, may I ask this - NMR experiments/pulse sequences are available to assign aromatic sidechains - Phe, Tyr, Trp? We'd like to try 2D and 3D.
What's available in the vendor-specific libraries?
Thank you very much.
Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
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