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The peptide amide protons exhibited NH i → Hα i −1 and NH i → Hα i NOEs (subscript i represents residue number) to the Hα protons.
It should be pointed out that although NOEs are invaluable in biomolecular structure determination their two potential drawbacks are: (i) NOEs only report on the local structure and (ii) their interpretation in flexible systems is notoriously difficult (Neuhaus and Williamson 2000).
A decrease of ∼50% in the intensity of the sequential dαN(i 1, i) NOEs for residues V3 and F4 increases the NOE intensity ratio to >0.5, consistent with a shift to an increased population of helical backbone angles compared to random coil.
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I– no.
(i) No singularity.
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