Nuclear magnetic resonance (NMR) relaxation times provide detailed information about molecular motions and local chemical environments. Longitudinal T(1) relaxation time is most often sensitive to relatively fast, nano- to picosecond ranges of molecular motion. Rotating frame T(1?) relaxation time reflects a much slower, micro- to millisecond range of motion, and the motional regime can be tuned by changing spin-lock field strength. Conventional methods for measuring T(1) and T(1?) relaxation...
[NMR paper] Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR
Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR
Protein dynamics are an intrinsically important factor when considering a protein's biological function. Understanding these motions is often limited through the use of static structure determination methods, namely, X-ray crystallography and cryo-EM. Molecular simulations have allowed for the prediction of global and local motions of proteins from these static structures. Nevertheless, determining local dynamics at residue-specific resolution through direct measurement remains crucial....
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03-28-2023 08:32 AM
[NMR paper] Accurate and Cost-Effective NMR Chemical Shift Predictions for Nucleic Acids Using a Molecules-in-Molecules Fragmentation-Based Method
Accurate and Cost-Effective NMR Chemical Shift Predictions for Nucleic Acids Using a Molecules-in-Molecules Fragmentation-Based Method
We have developed, implemented, and assessed an efficient protocol for the prediction of NMR chemical shifts of large nucleic acids using our molecules-in-molecules (MIM) fragment-based quantum chemical approach. To assess the performance of our approach, MIM-NMR calculations are calibrated on a test set of three nucleic acids, where the structure is derived from solution-phase NMR studies. For DNA systems with multiple conformers, the one-layer MIM method...
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01-12-2023 02:17 PM
[NMR paper] Accurate and cost-effective NMR chemical shift predictions for proteins using a molecules-in-molecules fragmentation-based method.
Accurate and cost-effective NMR chemical shift predictions for proteins using a molecules-in-molecules fragmentation-based method.
Related Articles Accurate and cost-effective NMR chemical shift predictions for proteins using a molecules-in-molecules fragmentation-based method.
Phys Chem Chem Phys. 2020 Nov 27;:
Authors: Chandy SK, Thapa B, Raghavachari K
Abstract
We have developed an efficient protocol using our two-layer Molecules-in-Molecules (MIM2) fragmentation-based quantum chemical method for the prediction of NMR chemical...
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11-29-2020 08:12 AM
Molecules - Special Issue “Hyperpolarized Molecules for Applications in Chemistry and Biomedicine”
From The DNP-NMR Blog:
Molecules - Special Issue “Hyperpolarized Molecules for Applications in Chemistry and Biomedicine”
Dear Colleagues,
I am pleased to announce that the journal Molecules (ISSN 1420-3049, IF 3.098) is currently running an NMR-related special issue entitled "Hyperpolarized Molecules for Applications in Chemistry and Biomedicine". Molecules is fully open access and is a partner of the Swiss Chemical Society. Open access is supported by the authors and their institutes, and an Article Processing Charge (APC) of 1800 CHF applies to accepted papers.
[NMR paper] Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph
Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
Biochemistry. 1997 Apr 8;36(14):4118-24
Authors: Olejniczak ET, Zhou MM, Fesik SW
Proteins recognize...
nmrlearner
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08-22-2010 03:31 PM
[NMR paper] Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph
Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
Biochemistry. 1997 Apr 8;36(14):4118-24
Authors: Olejniczak ET, Zhou MM, Fesik SW
Proteins recognize...
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08-22-2010 03:03 PM
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Si
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
Related Articles Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
J Am Chem Soc. 2010 Aug 6;
Authors: Krushelnitsky A, Zinkevich T, Reichert D, Chevelkov V, Reif B
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic...
Ultrafast T(1)-T(1rho) NMR for Correlating Different Motional Regimes of Molecules
Linear Mode
