but also 3 D and 4D). The typical protocol for protein structure determination by NMR proceeds as follows. Firstly, the chemical shifts observed on multidimensional spectra are assigned to their
NMR CHART “deshielded“ protons appear at low field highly shielded protons appear at high field deshielding moves proton resonance to lower field Electronegativity Dependence of Chemical Shift Dependence of the Chemical Shift of CH3X on the Element X Compound CH3X CH3F CH3OH CH3Cl CH3Br CH3I ...
To our surprise, the 1H NMR spectra of the borylporphyrin products 2a, 3a, and 4a indicated that borylation took place at the β-position adjacent to the unsubstituted meso-position. Typically, in the case of 2a, substantial downfield shifts due to the introduced boryl group were observed ...
NMR spectroscopy again confirmed that the structures of the wild type and mutants are not significantly affected by the deletions (Supplementary Fig. 9b). The effect of deleting loop-4 is particularly interesting as the equivalent region of KdHpuA, albeit being three residues shorter, is not ...