[ASAP] Cyanylated Cysteine Reports Site-Specific Changes at Protein–Protein-Binding Interfaces Without Perturbation
Cyanylated Cysteine Reports Site-Specific Changes at Protein–Protein-Binding Interfaces Without Perturbation
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00283/20180605/images/medium/bi-2018-00283c_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00283
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06-11-2018 07:38 PM
[NMR paper] Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
Related Articles Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
J Med Chem. 2017 Sep 14;:
Authors: Geist L, Mayer M, Cockcroft XL, Wolkerstorfer B, Kessler D, Engelhardt H, McConnell DB, Konrat R
Abstract
Fragment-based drug design exploits initial screening of low molecular weight compounds and their concomitant affinity improvement. The multitude of possible chemical...
nmrlearner
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09-15-2017 08:41 PM
Using Ligand-Induced Protein Chemical Shift PerturbationsTo Determine Protein–Ligand Structures
Using Ligand-Induced Protein Chemical Shift PerturbationsTo Determine Protein–Ligand Structures
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00170/20170427/images/medium/bi-2017-001707_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00170
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nmrlearner
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04-27-2017 05:44 PM
[NMR paper] Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.
Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.
Related Articles Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.
Molecules. 2015;20(12):21992-9
Authors: Ferrage F, Dutta K, Cowburn D
Abstract
The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology....
nmrlearner
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12-28-2015 12:26 AM
Hyperpolarized Water to Study Protein–Ligand Interactions
From The DNP-NMR Blog:
Hyperpolarized Water to Study Protein–Ligand Interactions
Chappuis, Q., et al., Hyperpolarized Water to Study Protein–Ligand Interactions. The Journal of Physical Chemistry Letters, 2015. 6(9): p. 1674-1678.
http://dx.doi.org/10.1021/acs.jpclett.5b00403
nmrlearner
News from NMR blogs
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06-06-2015 12:01 PM
[NMR paper] Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Related Articles Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Soft Matter. 2014 Feb 7;10(5):773-785
Authors: Ukpebor OT, Shah A, Bazov E, Boutis GS
Abstract
Using deuterium 2D T1-T2 Inverse Laplace Transform (ILT) NMR we have investigated the distribution, population, and...
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02-11-2014 09:58 PM
[Question from NMRWiki Q&A forum] bulk water relaxation dependence on temperature
bulk water relaxation dependence on temperature
Is liquid water's relaxation rate strongly dependent on temperature, and does anyone have a link to a good online article with the dependency equation?Thanks!
Check if somebody has answered this question on NMRWiki QA forum
nmrlearner
News from other NMR forums
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12-23-2011 10:21 AM
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...