[NMR paper] Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
Related ArticlesDifferences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
Biochim Biophys Acta. 2014 Feb 28;
Authors: Keppler JK, Sönnichsen FD, Lorenzen PC, Schwarz K
Abstract
The structure of ?-lactoglobulin (?-LG) is well characterized, but the exact location of binding sites for retinol and (-)-epigallocatechingallate (EGCG) are still a subject of controversy. Here we report that the genetic ?-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and ?-LG A with the most binding sites for EGCG, which include Tyr(20), Phe(151)and His(59). Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of ?-LG as nanotransporter.
PMID: 24590114 [PubMed - as supplied by publisher]
[NMR paper] Metabolic expressivity of human genetic variants: NMR metabotyping of MEN1 pathogenic mutants.
Metabolic expressivity of human genetic variants: NMR metabotyping of MEN1 pathogenic mutants.
Related Articles Metabolic expressivity of human genetic variants: NMR metabotyping of MEN1 pathogenic mutants.
J Pharm Biomed Anal. 2013 Oct 16;
Authors: Blaise BJ, Lopez C, Vercherat C, Lacheretz-Bernigaud A, Bayet-Robert M, Rezig L, Scoazec JY, Calender A, Emsley L, Elena-Herrmann B, Cordier-Bussat M
Abstract
Functional consequences of mutations in predisposition genes for familial cancer syndromes remain often elusive, especially when the...
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NMR and Fluorescence Studiesof Drug Binding to theFirst Nucleotide Binding Domain of SUR2A
NMR and Fluorescence Studiesof Drug Binding to theFirst Nucleotide Binding Domain of SUR2A
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi301019e/aop/images/medium/bi-2012-01019e_0008.gif
Biochemistry
DOI: 10.1021/bi301019e
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11-01-2012 10:38 PM
[NMR paper] Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubu
Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
Related Articles Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
Physiol Chem Phys Med NMR. 2001;33(2):139-51
Authors: Kuchroo K, Maity H, Kasturi SR
Tubulin, the major protein of microtubules, has been shown to be an example of protein undergoing multistep unfolding. Local unfolding and stepwise loss of a...
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11-19-2010 08:32 PM
[NMR paper] Protein folding and stability investigated by fluorescence, circular dichroism (CD),
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
Related Articles Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
J Biotechnol. 2000 May 26;79(3):281-98
Authors: van Mierlo CP, Steensma E
In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing...
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11-18-2010 09:15 PM
[NMR paper] Metal ion binding to calmodulin: NMR and fluorescence studies.
Metal ion binding to calmodulin: NMR and fluorescence studies.
Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.
Biometals. 1998 Sep;11(3):213-22
Authors: Ouyang H, Vogel HJ
Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad...
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11-17-2010 11:15 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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[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...
Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
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