Abstract
The dynamics of alanine methyl groups in alanine oligopeptides and polyalanine regions in Nephila clavata dragline and recombinant silks changed remarkably depending on the different packing arrangements. In particular, a notable difference in the 13C spin–lattice relaxation time T1 of Ala Cβ peaks was observed in the solid-state NMR between (Ala)6 and (Ala)7, which have rectangular and staggered packing arrangements, respectively. Moreover, the remarkably longer T1 value of the lowest field peak in Ala Cβ carbons clearly indicated the presence of staggered packing structure. Then, the relaxation behavior of polyalanine regions in spider dragline silks with mixed packing arrangements were clarified in both dry and hydrated states. The partial appearance of the staggered packing structure in (Ala)6 with rectangular packing structure was detected from the changes in line shapes of Ala 13Cβ peaks for the three kinds of 13C single-labeled (Ala)6 samples together with the change in their relaxation behavior.
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