Related ArticlesNMR study of the sites of human hemoglobin acetylated by aspirin.
Biochim Biophys Acta. 1999 Jul 13;1432(2):333-49
Authors: Xu AS, Macdonald JM, Labotka RJ, London RE
Acetylation of hemoglobin by aspirin and other acetylating agents has been used to generate hemoglobin analogs with altered structural and functional properties, and may prove useful in the treatment of sickle cell disease. We have studied the acetylation of human hemoglobin using [1'-(13)C]acetylsalicylic acid in combination with two-dimensional HMQC and HSQC NMR analysis. The spectra of the acetylated hemoglobin exhibit a number of well resolved resonances. Several spectral assignment strategies were used: blocking the 2, 3-DPG binding site non-covalently with inositol hexaphosphate or covalently with a cross-linking agent, selective carbamylation of the N-terminal valine amino groups with cyanate, spin-labeling the hemoglobin at betaCys93, and analysis of a hemoglobin triple mutant: betaV1MH2DeltaK144R, in which betaLys144 is replaced by an arginine residue. These studies support the conclusion that the most rapidly acetylated residue is betaLys82 rather than betaLys144, as previously reported. Further, it is apparent that acetyl betaLys82 can give rise to several resonances due to additional acetylation of betaLys82' or other nearby residues. An additional assignment strategy involving comparison of the chemical shifts of the acetyl resonances observed for adducts of diamagnetic carbonmonoxyhemoglobin with the shifts observed in paramagnetic cyanomethemoglobin provides information about the location of the acetyl derivatives relative to the heme irons. This approach is limited, however, by the lack of well defined structural information for the lysine residues on the protein surface. Additional tentative assignments have also been made, using the above approaches.
[NMR paper] Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Related Articles Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Biochim Biophys Acta. 2005 Sep 25;1741(3):339-49
Authors: Layden BT, Abukhdeir AM, Malarkey C, Oriti LA, Salah W, Stigler C, Geraldes CF, Mota de Freitas D
Li(+) binding in subcellular fractions of human...
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[NMR paper] Identification of platination sites on human serum transferrin using (13)C and (15)N
Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy.
Related Articles Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy.
J Biol Inorg Chem. 1999 Oct;4(5):621-31
Authors: Cox MC, Barnham KJ, Frenkiel TA, Hoeschele JD, Mason AB, He QY, Woodworth RC, Sadler PJ
Reactions between various apo and metal-bound forms of human serum transferrin (80 kDa) and the recombinant N-lobe (40 kDa) with or cis- have been investigated in solution via observation...
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NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...
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[NMR paper] 1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells
1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.
Biophys J. 1995 Feb;68(2):681-93
Authors: Fetler BK, Simplaceanu V, Ho C
Using improved selective excitation methods for protein nuclear...
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[NMR paper] 19F NMR study of the myosin and tropomyosin binding sites on actin.
19F NMR study of the myosin and tropomyosin binding sites on actin.
Related Articles 19F NMR study of the myosin and tropomyosin binding sites on actin.
Biochemistry. 1990 Feb 6;29(5):1348-54
Authors: Barden JA, Phillips L
Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization . Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum...
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[NMR paper] Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the inte
Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the...
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[NMR paper] An NMR analysis of the reaction of ubiquitin with [acetyl-1-13C]aspirin.
An NMR analysis of the reaction of ubiquitin with aspirin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An NMR analysis of the reaction of ubiquitin with aspirin.
Biochem Pharmacol. 1999 Jun 1;57(11):1233-44
Authors: Macdonald JM, LeBlanc DA, Haas AL, London RE
The acetylation of ubiquitin by aspirin has been studied using 2D NMR methods. Studies performed in a 50:50 H2O:D2O medium show doubling of the acetyl carbonyl resonances, indicating that all of the stable...