Journal ArticleDOI
Saturation transfer difference nuclear magnetic resonance study on the specific binding of ligand to protein.
TLDR
STD NMR method to map the group epitope and to measure the dissociation constant (K(D)) of specific interaction between ligand and protein is presented and results agree well with other reports of Trp-HSA interaction.About:
This article is published in Analytical Biochemistry.The article was published on 2009-02-15. It has received 37 citations till now. The article focuses on the topics: Ligand (biochemistry) & Nuclear magnetic resonance spectroscopy.read more
Citations
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Journal ArticleDOI
Saturation-Transfer Difference (STD) NMR: A Simple and Fast Method for Ligand Screening and Characterization of Protein Binding
TL;DR: This experiment is ideal to illustrate some fundamental NMR concepts, such as the nuclear Overhauser effect and relaxation in a multidisciplinary context, bridging chemistry and biochemistry with a taste of medicinal chemistry.
Journal ArticleDOI
NMR-based analysis of protein–ligand interactions
TL;DR: Three major ligand-observed NMR methods that depend on the nuclear Overhauser effect Spectroscopy, saturation transfer difference spectroscopy and water–ligand interactions observed via gradient spectroscopic experiments are reviewed with the aim of reporting recent developments and applications for the characterization of protein–ligands complexes, including affinity measurements and structural determination.
Journal ArticleDOI
Development of pyrazolone and isoxazol-5-one cambinol analogues as sirtuin inhibitors.
Sumit Mahajan,Michele Scian,Smitha Sripathy,Jeff Posakony,Uyen Lao,Taylor K. Loe,Vid Leko,Angel Thalhofer,Aaron D. Schuler,Antonio Bedalov,Julian A. Simon +10 more
TL;DR: In vitro cytotoxicity studies with these compounds as well as EX527, a potent and selective SIRT1 inhibitor, suggest that antilymphoma activity of this compound class may be predominantly due to SIRT2 inhibition.
Journal ArticleDOI
Direct STD NMR Identification of β‐Galactosidase Inhibitors from a Virtual Dynamic Hemithioacetal System
TL;DR: The direct in situ 1H STD-NMR identification of the best dynamic beta-galactosidase inhibitors from the dynamic HTA system was performed and the results were confirmed by inhibition studies, and the HTA product formed from the reaction between 1-thiogalactopyranose and a pyridine carboxaldehyde derivative provided the bestynamic inhibitor.
Journal ArticleDOI
Recent developments and applications of saturation transfer difference nuclear magnetic resonance (STD NMR) spectroscopy
TL;DR: It is illustrated that STD NMR is not simply a method for drug screening and discovery, but has qualitative and quantitative applications that can answer fundamental and applied biological and biomedical questions involving molecular interactions between ligands and proteins.
References
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Journal ArticleDOI
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
Moriz Mayer,Bernd Meyer +1 more
TL;DR: Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein.
Journal ArticleDOI
Group Epitope Mapping by Saturation Transfer Difference NMR To Identify Segments of a Ligand in Direct Contact with a Protein Receptor
Moriz Mayer,Bernd Meyer +1 more
TL;DR: Analysis of STD NMR experiments performed under competitive conditions proved that the two saccharides studied bind at the same receptor site, thereby ruling out unspecific binding.
Journal ArticleDOI
NMR Spectroscopy Techniques for Screening and Identifying Ligand Binding to Protein Receptors
Bernd Meyer,Thomas Peters +1 more
TL;DR: The approaches discussed in this review allow screening of compound libraries as well as a detailed identification of the groups involved in the binding events.
Journal ArticleDOI
The specific binding of L-tryptophan to serum albumin.
Rapier H. McMenamy,J.L. Oncley +1 more
TL;DR: An investigation was undertaken to determine which structural features of tryptophan are responsible for its binding, and to elucidate the nature of the binding site of the protein.
Journal ArticleDOI
Improved WATERGATE Pulse Sequences for Solvent Suppression in NMR Spectroscopy
TL;DR: Modifications to the WATERGATE method for removing the solvent resonance from H-1 NMR spectra provide narrower noninversion regions and hence enhance the sensitivities of the peaks close to the water resonance.
Related Papers (5)
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
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NMR Spectroscopy Techniques for Screening and Identifying Ligand Binding to Protein Receptors
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Group Epitope Mapping by Saturation Transfer Difference NMR To Identify Segments of a Ligand in Direct Contact with a Protein Receptor
Moriz Mayer,Bernd Meyer +1 more