For decades, numerous studies have attempted to understand intrinsic backbone preferences of amino-acids and find intermolecular forces relating to neighboring effects in short peptides and denatured proteins. In order to investigate the comprehensive preferences of side chain properties and denatured proteins, we performed spectroscopic study and analysis especially NMR scalar coupling constants and chemical shifts of a complete 400 blocked dipeptides set, as many as possible in dipeptide systems. Surprisingly, although the systems have chemical diversities of side-chain properties, backbone conformational and environmental distributions are greatly narrow and similar. In addition, it is worth noticing that similarity between dipeptides and denatured proteins. For the understanding of unfolded state, present dipeptides library can be model peptides as system containing structural and environmental information of denatured proteins.

Intrinsic backbone conformational propensities of a complete set of blocked diptptides: Comparisons with denatured proteins

243rd National Meeting (2012)

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