Diffusion nuclear magnetic resonance spectroscopy detects substoichiometric concentrations of small molecules in protein samples

Analytical Biochemistry

Volumn 396, Issue 1, 2010, Pages 117-123

  Ribeiro, João P ^a   Palczewska, Małgorzata ^b,c   André, Sabine ^d   Cañada, F Javier ^a   Gabius, Hans Joachim ^d   Jiménez Barbero, Jesús ^a   Mellström, Britt ^c   Naranjo, José R ^c   Scheffers, Dirk Jan ^b   Groves, Patrick ^a,b  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^c CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^d UNIVERSITY OF MUNICH   (Germany)

Author keywords

Contamination; Diffusion; DOSY; Lectin; Protein purification; Relaxation

Indexed keywords

AFFINITY CHROMATOGRAPHY; CONTAMINATION; DIFFUSION; DRUG PRODUCTS; HIGH PRESSURE LIQUID CHROMATOGRAPHY; ION EXCHANGE; MASS SPECTROMETRY; MOLECULES; NUCLEAR MAGNETIC RESONANCE; PROTEINS; REAGENTS;

DOSY; FLUORESCENT REAGENT; LECTIN; NUCLEAR MAGNETIC RESONANCE(NMR); PROTEIN PURIFICATION; RELAXATION; SAMPLE MANIPULATION; SAMPLE PREPARATION PROCEDURE;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

ALPHA LACTALBUMIN; BOVINE SERUM ALBUMIN; CALSENILIN; CARBONATE DEHYDRATASE; IMIDAZOLE; LECTIN;

ARTICLE; CONCENTRATION PROCESS; CONTROLLED STUDY; FEASIBILITY STUDY; HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; RELIABILITY; SENSITIVITY ANALYSIS; STOICHIOMETRY;

EID: 70449674249     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.09.001     Document Type: Article

References (27)

1. Altria K., Marsh A., and Sänger-van de Griend C. Capillary electrophoresis for the analysis of small-molecule pharmaceuticals. Electrophoresis 27 (2006) 2263-2282
2. Jiang Y., Wang P.C., Locascio L.E., and Lee C.S. Integrated plastic microfluidic devices with ESI-MS for drug screening and residue analysis. Anal. Chem. 73 (2001) 2048-2053
3. Stilbs P. Molecular self-diffusion coefficients in Fourier transform nuclear magnetic resonance spectrometric analysis of complex mixtures. Anal. Chem. 53 (1981) 2135-2137
4. Johnson Jr. C.S. Diffusion ordered NMR spectroscopy: principles and applications. Prog. NMR Spectrosc. 34 (1999) 203-256
5. Cobas J.C., Groves P., Martín-Pastor M., and De Capua A. New applications, processing methods, and pulse sequences using diffusion NMR. Curr. Anal. Chem. 1 (2005) 289-305
6. Groves P., Palczewska M., Molero M.D., Batta G., Cañada F.J., and Jiménez-Barbero J. Protein molecular weight standards can compensate systematic errors in diffusion ordered spectroscopy. Anal. Biochem. 331 (2004) 395-397
7. 1H NMR spectroscopy of biological fluids. Anal. Chem. 68 (1996) 3370-3376
8. 1H NMR spectra of organic compounds. J. Org. Chem. 71 (2006) 4103-4110
9. Politi M., Groves P., Chávez M.I., Cañada F.J., and Jiménez-Barbero J. Useful applications of DOSY experiments for the study of mushroom polysaccharides. Carbohydr. Res. 341 (2006) 84-89
10. Brand T., Cabrita E.J., and Berger S. Intermolecular interaction as investigated by NOE and diffusion studies. Prog. NMR Spectrosc. 46 (2005) 159-196
11. 1H NMR spectroscopy of biological fluids. Anal. Chem. 68 (1996) 3370-3376
12. Otto W.H., and Larive C.K. Improved spin-echo-edited NMR diffusion measurements. J. Magn. Reson. 153 (2001) 273-276
13. Becker B.A., Morris K.F., and Larive C.K. An improved method for suppressing protein background in PFG NMR experiments to determine ligand diffusion coefficients in the presence of receptor. J. Magn. Reson. 181 (2006) 327-330
14. López-Lucendo M.F., Solís D., André S., Hirabayashi J., Kasai K.-I., Kaltner H., Gabius H.-J., and Romero A. Growth-regulatory human galectin-1: crystallographic characterization of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 343 (2004) 957-970
15. André S., Pei Z., Siebert H.-C., Ramström O., and Gabius H.-J. Glycosyldisulfides from dynamic combinatorial libraries as O-glycoside mimetics for plant and endogenous lectins: their reactivities in solid-phase and cell assays and conformational analysis by molecular dynamics simulations. Bioorg. Med. Chem. 14 (2006) 6314-6326
16. Kaltner H., Solís D., Kopitz J., Lensch M., Lohr M., Manning J.C., Mürnseer M., Schnölzer M., André S., Sáiz J.L., and Gabius H.-J. Prototype chicken galectins revisited: characterization of a third protein with distinctive hydrodynamic behaviour and expression pattern in organs of adult animals. Biochem. J. 409 (2008) 591-599
17. López-Lucendo M.F., Solís D., Sáiz J.L., Kaltner H., Russwurm R., André S., Gabius H.-J., and Romero A. Homodimeric chicken galectin CG-1B (C-14): crystal structure and detection of unique redox-dependent shape changes involving inter- and intrasubunit disulfide bridges by gel filtration, ultracentrifugation, site-directed mutagenesis, and peptide mass fingerprinting. J. Mol. Biol. 386 (2009) 366-378
18. André S., Kaltner H., Lensch M., Russwurm R., Siebert H.-C., Fallsehr C., Tajkhorschid E., Heck A.J.R., von Knebel-Doeberitz M., Gabius H.-J., and Kopitz J. Determination of structural and functional overlap/divergence of five proto-type galectins by analysis of the growth-regulatory interaction with ganglioside GM1 in silico and in vitro on human neuroblastoma cells. Int. J. Cancer 114 (2005) 46-57
19. Scheffers D.J. The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA. FEBS Lett. 582 (2008) 2601-2608
20. Löwe J., and Amos L.A. Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes. Int. J. Biochem. Cell Biol. 41 (2009) 323-329
21. Marion D., Ikura M., and Bax A. Improved solvent suppression in one-dimensional and two-dimensional NMR spectra by convolution of time-domain data. J. Magn. Reson. 84 (1989) 425-430
22. Gabius H.-J., Siebert H.-C., André S., Jiménez-Barbero J., and Rüdiger H. Chemical biology of the sugar code. ChemBioChem 5 (2004) 740-764
23. In: Gabius H.-J. (Ed). The Sugar Code: Fundamentals of Glycosciences (2009), Wiley-VCH, Weinheim, Germany
24. Gabius H.-J. Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands. Anal. Biochem. 189 (1990) 91-94
25. 2+-regulated transcriptional repressor. Nature 398 (1999) 80-84
26. 2+ differentially regulate DNA binding and dimerization of DREAM. J. Biol. Chem. 280 (2005) 18008-18014
27. Huecas S., Schaffner-Barbero C., García W., Yébenes H., Palacios J.M., Díaz J.F., Menéndez M., and Andreu J.M. The interactions of cell division protein FtsZ with guanine nucleotides. J. Biol. Chem. 282 (2007) 37515-37528