Exchange enhanced sensitivity gain for solvent-exchangeable protons in 2D H-1-N-15 heteronuclear correlation spectra acquired with band-selective pulses
Details
Publication Year 2011-08,Volume 211,Issue #2,Page 243-247
Journal Title
JOURNAL OF MAGNETIC RESONANCE
Publication Type
Journal Article
Abstract
Conformational or chemical exchange can cause significant sensitivity loss in NMR spectroscopy through resonance broadening for nuclear spins involved in these processes. While this effect may sometimes be alleviated by manipulating experimental conditions such as temperature, pH, and buffers, conditions optimal for all resonances are not always achievable. As a consequence, any means of recovering or minimizing this exchange-induced sensitivity loss is potentially of significant value in regaining information otherwise lost. We report the experimental observation of significant sensitivity gain for nuclear spins undergoing chemical exchange with solvent (water) at exchange rates ca 1-10 s(-1) in H-1-N-15 correlation spectra of proteins acquired with band-selective pulses (the SOFAST-HMQC sequence). (C) 2011 Elsevier Inc. All rights reserved.
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
PROTEIN NMR EXPERIMENTS; CHEMICAL-EXCHANGE; SPECTROSCOPY; RECONSTRUCTION; TEMPERATURE; ACQUISITION; SECONDS; SCHEME
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2011-08-01 12:00:00
An error has occurred. This application may no longer respond until reloaded. Reload 🗙