I have solved the structure of a alpha-helical peptide, containing 27 residues, bound to micelles. I had to cut of six amino acids (from 33) because of overlap. CD spectroscopy helped to give some hints about secondary structure formation.
But, it all depends on the spectra quality. I think for a non membrane bound peptide noesy/tocsy spectra and even cosy should look very nice. If the work is very important, partially 15N labelling might be helpfull.
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