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G. Jung, M. Ottnad (1974)
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H\c,s-s -OOC-CH qH HI ' CH-HN I' H \ N-C ,' (1) This peptide, containing an intramolecular S-S bond, has been fully studied by means of the x-ray method.' This analysis shows that in the solid state, the molecule contains a cis peptide unit and a right-handed helical sense of the disulfide group. On the other hand, earlier predictions based on potential energy calculations2 gave two most-probable conformations, which differ from each other mainly in the opposite chirality of the disulfide bridge (ca. f90'). One of the predicted conformations is very close to that found in the solid state. The absence of optical activity in the region of long-wavelength disulfide absorption3 is consistent with a dihedral angle of the disulfide group in solution of ca. More detailed and somewhat complementary information on the structure of this molecule in solution can be obtained by means of the nmr technique. Here w e report a conformational analysis of I by means of lH-nmr. EXPERIMENTAL Peptide (I) was synthesized according to the method described by Izumiya and Green~tein.~ I t was purified by gel-filtration chromatography using a Sephadex (2-10 column eluted with 0.02M NH4HC03 and then crystallized from water. 'H-nmr spectra
Biopolymers – Wiley
Published: Jun 1, 1979
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