Nuclear magnetic resonance (NMR) spectroscopy allows studying proteins in solution and under physiological temperatures. Frequently, either the amide groups of the protein backbone or the methyl groups in side chains are used as reporters of structural dynamics in proteins. A structural dynamics study of the protein backbone of globular proteins on ^(15)N labeled and fully protonated samples usually works well for proteins with a molecular weight of up to 50 kDa. When side chain deuteration in...
[NMR paper] Rapid Characterization of Structural and Behavioral Changes of Therapeutic Proteins by Relaxation and Diffusion (1)H-SOFAST NMR Experiments
Rapid Characterization of Structural and Behavioral Changes of Therapeutic Proteins by Relaxation and Diffusion (1)H-SOFAST NMR Experiments
Biologic drugs have emerged as a rapidly expanding and important modality, offering promising therapeutic solutions by interacting with previously "undruggable" targets, thus significantly expanding the range of modern pharmaceutical applications. However, the inherent complexity of these drugs also introduces liabilities and poses challenges in their development, necessitating efficient screening methods to evaluate the structural stability and...
[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
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05-01-2018 10:57 PM
[NMR paper] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Related Articles Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Biochemistry. 2018 Apr 17;:
Authors: Baird-Titus JM, Thapa M, Doerdelmann T, Combs KA, Rance M
Abstract
An important but poorly characterized contribution to the thermodynamics of protein-DNA interactions is...
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04-18-2018 01:41 PM
[NMR paper] Characterizing Protein Dynamics with NMR R 1? Relaxation Experiments.
Characterizing Protein Dynamics with NMR R 1? Relaxation Experiments.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Characterizing Protein Dynamics with NMR R 1? Relaxation Experiments.
Methods Mol Biol. 2018;1688:205-221
Authors: Massi F, Peng JW
Abstract
The measurement of R1? , the longitudinal relaxation rate constant in the rotating frame, is one of the few available methods to characterize the ?s-ms functional dynamics...
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11-21-2017 10:10 PM
Practical considerations for investigation of protein conformational dynamics by 15 N R 1Ï? relaxation dispersion
Practical considerations for investigation of protein conformational dynamics by 15 N R 1Ï? relaxation dispersion
Abstract
It is becoming increasingly apparent that proteins are not static entities and that their function often critically depends on accurate sampling of multiple conformational states in aqueous solution. Accordingly, the development of methods to study conformational states in proteins beyond their ground-state structure (â??excited statesâ??) has crucial biophysical importance. Here we investigate experimental schemes for optimally...
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03-01-2017 04:13 AM
[NMR paper] Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
Related Articles Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
J Phys Chem B. 2014 Oct 28;
Authors: Allnér O, Foloppe N, Nilsson L
Abstract
Molecular dynamics simulations of E. coli glutaredoxin1 in water have been performed to relate the dynamical parameters and entropy obtained in NMR relaxation experiments, with results extracted from simulated trajectory...
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10-29-2014 03:51 PM
[NMR paper] Investigation of proteins in living bacteria with in-cell NMR experiments.
Investigation of proteins in living bacteria with in-cell NMR experiments.
Related Articles Investigation of proteins in living bacteria with in-cell NMR experiments.
Top Curr Chem. 2008;273:203-14
Authors: Dötsch V
Abstract
In recent years NMR methods have been developed that enable the observation of proteins insideliving bacterial cells. Because of the sensitivity of the chemical shift to environmental changesthese in-cell NMR experiments can be used to study protein conformation, molecular interaction ordynamics in a*protein's natural...
NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Linear Mode
