Abstract
Solution-state NMR has been widely applied to determine the three-dimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.
PMID: 26361636 [PubMed - as supplied by publisher]
[NMR paper] A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Related Articles A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Eur J Med Chem. 2014 Jun 11;83C:92-101
Authors: Sim?i? M, Pureber K, Kristan K, Urleb U, Kocjan D, Grdadolnik SG
Abstract
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide,...
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A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
Publication date: Available online 11 June 2014
Source:European Journal of Medicinal Chemistry</br>
Author(s): Mihael Sim?i? , Kaja Pureber , Katja Kristan , Uroš Urleb , Darko Kocjan , Simona Goli? Grdadolnik</br>
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide, an 2-oxoindolinylidene derivative with novel structure scaffold, was evaluated for inhibition potency...
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[NMR paper] Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies.
Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies.
Related Articles Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies.
ScientificWorldJournal. 2014;2014:656201
Authors: Peana MF, Medici S, Ledda A, Nurchi VM, Zoroddu MA
Abstract
P1D2E3K4H5E6L7 (PK9-H), a fragment of Ypk9, the yeast homologue of the human Park9 protein, was studied for its coordination abilities towards Ni(II) and Cu(II) ions through mono- and bi-dimensional NMR techniques. Both proteins are involved in the...
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[NMR paper] NMR studies on protein-nucleic acid interaction.
NMR studies on protein-nucleic acid interaction.
Related Articles NMR studies on protein-nucleic acid interaction.
J Biomol NMR. 2013 May 9;
Authors: Kaptein R
Abstract
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[NMR paper] NMR investigation of the interaction of the inhibitor protein Im9 with its partner DN
NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase.
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Protein Sci. 2000 Sep;9(9):1709-18
Authors: Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR
The bacterial toxin colicin E9 is secreted by producing Escherichia coli cells with its 9.5 kDa inhibitor protein Im9 bound tightly to its 14.5 kDa C-terminal DNase domain. Double- and triple-resonance NMR spectra of the 24 kDa...
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[NMR paper] Characterization of the interaction between bovine pancreatic trypsin inhibitor and t
Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR.
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Biophys Chem. 1998 Apr 20;71(2-3):221-34
Authors: Jolivalt C, Böckmann A, Riès-Kautt M, Ducruix A, Guittet E
The interaction between Bovine Pancreatic Trypsin Inhibitor and thiocyanate was studied using NMR spectroscopy following several experimental approaches. The chemical shift variations of the BPTI protons in the...
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[NMR paper] Carbohydrate-protein interaction studies by laser photo CIDNP NMR methods.
Carbohydrate-protein interaction studies by laser photo CIDNP NMR methods.
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Glycoconj J. 1997 Jun;14(4):531-4
Authors: Siebert HC, Kaptein R, Beintema JJ, Soedjanaatmadja UM, Wright CS, Rice A, Kleineidam RG, Kruse S, Schauer R, Pouwels PJ, Kamerling JP, Gabius HJ, Vliegenthart JF
The side chains of tyrosine, tryptophan and histidine are able to produce CIDNP (Chemically Induced Dynamic Nuclear Polarization) signals after laser irradiation in the...
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[NMR paper] NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosa
NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
Biochem Pharmacol. 1990 Jul 1;40(1):65-8
Authors: Petros AM, Kopple KD
Protein-Inhibitor Interaction Studies Using NMR.
Linear Mode
