Related ArticlesLactic acid and protein interactions: implications for the NMR visibility of lactate in biological systems.
Biochim Biophys Acta. 1999 Jan 4;1426(1):177-84
Authors: Chatham JC, Forder JR
The addition of bovine serum albumin (BSA) to a solution of lactate and alanine resulted in the disappearance of the 1H-NMR resonances from lactate but not alanine. As temperature is increased lactate becomes increasingly NMR visible and after heating above 65 degreesC and cooling to 25 degreesC lactate binding is reduced. With a concentration of 0.2 mM BSA, there was a linear relationship between NMR visible lactate versus total lactate over a range of lactate concentrations of 0.2-35 mM (slope 0.384+/-0.003) indicating that approx. 60% of the added lactate is not visible in the 1H-NMR spectrum. With a 0.1 mM BSA solution, however, the slope was markedly higher indicating that under these conditions only 25-30% of the lactate was NMR invisible. The results from this study indicate that decreased NMR visibility of lactate in proteinaceous solutions is due to non-specific binding which is dependent on the tertiary structure of the protein. This has important implications not only for the interpretation of in vivo 1H-NMR experiments but also for 13C, and 14C studies of metabolism.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Protein Sci. 2011 Feb;20(2):327-35
Authors: Basehore HK, Ropson IJ
The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak...
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Fluorine-Protein Interactions and (19)F NMR Isotropic Chemical Shifts: An Empirical Correlation with Implications for Drug Design.
Fluorine-Protein Interactions and (19)F NMR Isotropic Chemical Shifts: An Empirical Correlation with Implications for Drug Design.
Related Articles Fluorine-Protein Interactions and (19)F NMR Isotropic Chemical Shifts: An Empirical Correlation with Implications for Drug Design.
ChemMedChem. 2010 Nov 29;
Authors: Dalvit C, Vulpetti A
An empirical correlation between the fluorine isotropic chemical shifts, measured by (19)F NMR spectroscopy, and the type of fluorine-protein interactions observed in crystal structures is presented. The CF, CF(2), and...
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12-01-2010 04:41 PM
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Related Articles Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Protein Sci. 2010 Nov 29;
Authors: Basehore HK, Ropson IJ
The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19)F-NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak assignments...
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12-01-2010 04:41 PM
[NMR paper] Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures
Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us.
Related Articles Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us.
Prog Lipid Res. 2004 May;43(3):177-99
Authors: Hamilton JA
The interactions of fatty acids with proteins have been studied by a variety of conventional approaches for decades. However, only limited aspects of fatty acid-protein interactions have been elucidated, even with the integration of information gleaned from the many techniques....
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11-24-2010 09:51 PM
[NMR paper] NMR studies of protein-nucleic acid interactions.
NMR studies of protein-nucleic acid interactions.
Related Articles NMR studies of protein-nucleic acid interactions.
Methods Mol Biol. 2004;278:289-312
Authors: Varani G, Chen Y, Leeper TC
Protein-DNA and protein-RNA complexes play key functional roles in every living organism. Therefore, the elucidation of their structure and dynamics is an important goal of structural and molecular biology. Nuclear magnetic resonance (NMR) studies of protein and nucleic acid complexes have common features with studies of protein-protein complexes: the...
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11-24-2010 09:25 PM
[NMR paper] Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined b
Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Related Articles Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Protein Sci. 1998 Sep;7(9):1930-8
Authors: Kim S, Baum J
alpha-Lactalbumin (alpha-LA) undergoes a pH-dependent unfolding from the native state to a partially unfolded state (the molten globule state). To understand the role of electrostatic interactions in protein denaturation, NMR and CD pH titration experiments are performed on guinea pig...
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[NMR paper] A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2
A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2+, and the pH gradient.
Related Articles A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2+, and the pH gradient.
Biochemistry. 1992 Feb 11;31(5):1322-30
Authors: Hutson SM, Williams GD, Berkich DA, LaNoue KF, Briggs RW
The effects of external pH, temperature, and Ca2+ and Mn2+ concentrations on the compartmentation and NMR visibility of inorganic phosphate (Pi) were studied in isolated rat liver mitochondria respiring on...
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08-21-2010 11:41 PM
[NMR paper] 13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty ac
13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proteins produced in the intestinal epithelium.
Related Articles 13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proteins produced in the intestinal epithelium.
Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):101-10
Authors: Cistola DP, Sacchettini JC, Gordon JI
A high-resolution, solution-state NMR method for characterizing and comparing the interactions between carboxyl 13C-enriched fatty acids (FA) and...
Lactic acid and protein interactions: implications for the NMR visibility of lactate
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