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Fourier transform microwave spectroscopy of Ac Ser NH2: the role of side chain interactions in peptide folding

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Figure

Fig. 1  (a) Broadband spectrum of Ac-Ser-NH 2  in the 6–12 GHz frequency region showing the most intense rotational transitions for the observed
Fig. 2   The predicted five low-energy conformers of Ac-Ser-NH 2 .
Fig. 3  3D  ab  initio  structure  (Cartesian  coordinates  in  Table  S4  of  the  ESI†) of the observed conformer of Ac-Ser-NH 2  showing  the intra-

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