Related ArticlesHigh resolution NMR for screening ligand/protein binding.
Curr Opin Drug Discov Devel. 1999 Jul;2(4):396-400
Authors: Shapiro MJ, Wareing JR
High resolution NMR spectroscopy has provided a versatile tool for assessing ligand/receptor interactions. NMR-based methods are currently being investigated which may prove valuable for compound screening. These techniques include the use of chemical shift perturbations, the monitoring of translational diffusion and the observation of NOEs. Novel experiments like TROSY and NOE pumping will play significant roles in looking at proteins larger than 30 kDa. New probe technology such as the Cryoprobe could have a significant impact on NMR-based screening for drug discovery by lowering the necessary amount of (15)N-labled protein.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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01-18-2011 10:22 PM
[NMR paper] Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent p
Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Related Articles Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Arch Pharm (Weinheim). 2005 Jun;338(5-6):217-28
Authors: Luca S, Heise H, Lange A, Baldus M
Solid-state Nuclear Magnetic Resonance (NMR) provides a general method to study molecular structure and dynamics in a non-crystalline and insoluble environment. We discuss the latest methodological progress to...
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[NMR paper] Characterization of protein-ligand interactions by high-resolution solid-state NMR sp
Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
Related Articles Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Nov 3;126(43):13948-53
Authors: Zech SG, Olejniczak E, Hajduk P, Mack J, McDermott AE
A novel approach for detection of ligand binding to a protein in solid samples is described. Hydrated precipitates of the anti-apoptotic protein Bcl-xL show well-resolved (13)C-(13)C 2D solid-state NMR spectra that allow...
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11-24-2010 10:03 PM
[NMR paper] NMR spectroscopy techniques for screening and identifying ligand binding to protein r
NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors.
Related Articles NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors.
Angew Chem Int Ed Engl. 2003 Feb 24;42(8):864-90
Authors: Meyer B, Peters T
Binding events of ligands to receptors are the key for an understanding of biological processes. Gaining insight into protein-protein and protein-ligand interactions in solution has recently become possible on an atomic level by new NMR spectroscopic techniques....
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11-24-2010 09:01 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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08-22-2010 03:31 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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08-22-2010 03:03 PM
[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...
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08-22-2010 03:29 AM
[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Biochemistry. 1991 Jun 4;30(22):5524-31
Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...
High resolution NMR for screening ligand/protein binding.
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