[NMR paper] Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
J Am Chem Soc. 2016 Mar 14;
Authors: Chen WN, Nitsche C, Pilla KB, Graham B, Huber T, Klein CD, Otting G
Abstract
Structure-guided drug design relies on detailed structural knowledge of protein-ligand complexes, but crystallization of co-complexes is not always possible. Here we present a sensitive nuclear...
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03-15-2016 11:57 AM
[NMR paper] Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
J Med Chem. 2013 Oct 30;
Authors: Kodama Y, Takeuchi K, Shimba N, Ishikawa K, Suzuki EI, Shimada I, Takahashi H
Abstract
In this study, we developed an assignment-free approach for rapid identification of ligand-binding sites in target...
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11-01-2013 07:39 PM
[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):i
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Protein-ligand interactions are driven by many factors, including protein conformation and pH of the solution. Electrospray mass spectrometry can reveal the degree of protein folding from the distribution of...
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07-31-2013 12:00 PM
[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):895-903
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Human liver fatty acid binding protein (hL-FABP) is the most abundant cytosolic protein in the liver. This protein plays important roles associated to partitioning of fatty acids (FAs) to specific...
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Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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03-05-2011 01:02 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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[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...