Aggregation facilitates analysis: The Ca 2+-dependent mannose (Man) binding of the nonpeptidic carbohydrate binder pradimicinA (PRM-A) was investigated in the solid state. The use of PRM-A aggregates eliminated problems associated with the three-component equilibrium. A combination of 113CdNMR spectroscopy and 2D dipolar-assisted rotational resonance revealed the mannose-binding site of PRM-A and the crucial role of the Ca 2+ ion (see binding model).
|Number of pages||5|
|Journal||Angewandte Chemie - International Edition|
|Publication status||Published - 2011 Jun 27|
- natural products
- solid-state NMR spectroscopy
ASJC Scopus subject areas