High-resolution 15N NMR spectroscopy has been a well established and powerful tool for the study of structure and dynamics of peptides and proteins, especially since the introduction of the new pulsed magnetization transfer methods which permit proton detection. Solvent suppression is necessary when working in water with biological samples and is a serious problem in micelle-containing water solutions, where the water resonance is particularly broad. We report the study of a peptide in micelle solution at 15N natural abundance using reverse detection combined with an efficient solvent suppression scheme. This approach is particularly useful for those cases where isotopic substitution is prohibitively expensive and time consuming.
N-15 Reverse Detection of Little Gastrin In Micelle Solution
MAMMI, STEFANO
1990
Abstract
High-resolution 15N NMR spectroscopy has been a well established and powerful tool for the study of structure and dynamics of peptides and proteins, especially since the introduction of the new pulsed magnetization transfer methods which permit proton detection. Solvent suppression is necessary when working in water with biological samples and is a serious problem in micelle-containing water solutions, where the water resonance is particularly broad. We report the study of a peptide in micelle solution at 15N natural abundance using reverse detection combined with an efficient solvent suppression scheme. This approach is particularly useful for those cases where isotopic substitution is prohibitively expensive and time consuming.Pubblicazioni consigliate
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