Increasing sequence length favors alpha-helix over 3(10)-helix in alanine-based peptides: evidence for a length-dependent structural transition.
作者： Wayne R. Fiori , Siobhan M. Miick , Glenn L. Millhauser
DOI: 10.1021/BI00096A003
关键词:
摘要: Ala-based peptides form marginally stable helices at low temperature and are conventionally considered as mixtures of alpha-helix random coil. However, recent work with doubly spin-labeled suggests that short 16-residue sequences contain a significant fraction 3(10)-helix near the N-terminus (positions 4-8). Using same double-label strategy, we report on helix geometry Ac-(AAAAK)nA-NH2 n = 3 4. The 16-mer (n 3) is now examined region C-terminus, there evidence for here well. 21-mer 4) in three regions sequence. In dramatic contrast to 16-mer, exhibits signature through middle peptide. however, adopts often found C-termini protein alpha-helices. These data indicate proportion depends upon sequence length.
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