Abstract
Contrary to the view based on the classical random coil model, it is now clearly established that individual amino acid residues in unfolded peptides and proteins differ with regard to their conformational propensities. The prime example is alanine which shows a very high preference for polyproline II (pPII). Recently, our research groups conducted a conformational analysis of GxyG host-guest peptides with selected mixtures of aliphatic (A,V,L) and more polar/charged residues (S,D,K) as guest residues x and y.
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