Abstract
The ^(15)N NMR shifts of chemically and optically pure N- and C-protected homooligopeptides derived from L-norvaline and L-valine to the tetramers have been determined at the natural-abundance level of ^(15)N by using the Fourier-transform technique. The shift effects produced by increasing the chain length and temperature, as well as changing the solvent from a hydrogen-bonding donor to a hydrogen-bonding acceptor and replacing the linear side chain (as in the norvaline peptides) by a β branched side chain (as in the valine peptides), are discussed.
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