Change search
ReferencesLink to record
Permanent link

Direct link
PGSE-WATERGATE, a new tool for NMR diffusion-based studies of ligand-macromolecule binding
KTH, Superseded Departments, Chemistry.
2002 (English)In: Magnetic Resonance in Chemistry, ISSN 0749-1581, E-ISSN 1097-458X, Vol. 40, no 6, 391-395 p.Article in journal (Refereed) Published
Abstract [en]

A new pulsed gradient spin-echo NMR diffusion sequence, PGSE-WATERGATE, which is based on the extremely efficient WATERGATE solvent suppression sequence, is presented. The sequence is simple to set up and particularly suited to measuring the diffusion coefficients of small ligands in aqueous solution such as is commonly required in pharmaceutical and combinatorial applications. It also affords the possibility of measuring the diffusion of exchangeable resonances, which is often impossible in conjunction with other suppression schemes. Further, a trivial modification of the sequence affords the possibility of multiple solvent suppression, thereby increasing its suitability to LC-NMR applications. The utility of the sequence is demonstrated on the salicylate-bovine serum albumin system. The dissociation constant, K-d, and the number of binding sites were found to be 0.030 M and 33, respectively. Importantly, the extremely high degree of suppression provided by the new sequence allowed the salicylate diffusion coefficients to be measured over a very wide concentration range sufficient to show that the salicylate-bovine serum albumin system is not well described by a simple two-site model. Previous studies in the literature have been based on data from a smaller concentration range, for which this model gives an apparently good fit.

Place, publisher, year, edition, pages
2002. Vol. 40, no 6, 391-395 p.
Keyword [en]
NMR, H-1 NMR, albumin, binding, diffusion, PGSE, PGSE-WATERGATE, solvent suppression, spin-echo, WATERGATE, nuclear-magnetic-resonance, studying translational diffusion, pulsed-field gradients, human serum-albumin, stimulated-echo, signal suppression, spectroscopy, relaxation, temperature, excitation
URN: urn:nbn:se:kth:diva-21561DOI: 10.1002/mrc.1029ISI: 000175746300003OAI: diva2:340259
QC 20100525Available from: 2010-08-10 Created: 2010-08-10Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Stilbs, Peter
By organisation
In the same journal
Magnetic Resonance in Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 18 hits
ReferencesLink to record
Permanent link

Direct link