Answers are grounded in this paper and cite their sources.
Detailed and precise information on the exchanges in water of the peptide hydrogens of the insulin fragment B23-B29 (Gly23-Phe24-Phe25-Tyr26-Thr27-Pro28 -Lys29) has been obtained from magnetization-transfer measurements, and nonlinear least-squares fits of the experimental spectra using the expression for the discrete Fourier transform of a sum of exponentially damped sinusoids. From a comparison of the differential exchange rates with those expected for completely solvent-exposed peptide hydrogens, specific conformational features of the heptapeptide are suggested.
No takes yet. Share an insight, caveat, or question.
Abildgaard et al. (1989) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: