Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides

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Abstract

Practical aspects of the E.COSY technique for measurement of coupling constants are discussed. Guidelines are presented for the experimental setup and for spectral assignments. The features of E.COSY cross-peak multiplet patterns are illustrated by experimental spectra of valine, phenylalanine, and proline residues in the decapeptide antamanide.

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    In such situations, the accurate measurement of nJHH from the conventional 1D 1H spectrum is severely hindered. A number of two dimensional and modified 1D [8] experiments has been reported for the precise measurement of scalar couplings, viz., 2D COSY [9–11], DQF COSY [12], E-COSY [13], PCR-COSY [14], J-upscaled COSY [15,16], J-resolved [17–20] and SERF [21] techniques. The SERF [21] experiment based on selective excitation and J-resolved concept aids in the accurate measurement of nJHH.

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