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Comparative Study
. 1985 Jan;25(1):89-98.
doi: 10.1111/j.1399-3011.1985.tb02150.x.

Conformational analysis of cyclized dipeptide models for specific types of beta-bends by two-dimensional nuclear Overhauser spectroscopy

Comparative Study

Conformational analysis of cyclized dipeptide models for specific types of beta-bends by two-dimensional nuclear Overhauser spectroscopy

E R Stimson et al. Int J Pept Protein Res. 1985 Jan.

Abstract

The solution conformations in DMSO-d6 of the two cyclized dipeptides, cyclo(L-alanyl-L-alanyl-epsilon-aminocaproyl) and cyclo(L-alanyl-D-alanyl-epsilon-aminocaproyl), have been analyzed by means of the two-dimensional nuclear Overhauser effect (2D-NOE). The preferred conformations for the two compounds have been deduced by comparing proton-proton distances, derived from the 2D-NOE data and relaxation-time measurements, with the corresponding distances in several possible computed low-energy conformations. The predominant conformations are a type III bend and a type II bend, respectively, for the two compounds. These conclusions agree with those deduced earlier on the basis of infrared and Raman spectra and circular dichroism measurements.

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