Showing papers by "Gautam Basu published in 1992"
TL;DR: In this paper, the authors extended the analysis of the factors that control the helical folding of Aib-rich peptides to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib alpha-mono-alkylated residues.
Abstract: The analysis of the factors that control the helical folding of Aib-rich peptides is extended to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib alpha-mono-alkylated residues. The distinct hydrogen-bonding network of the 3(10)-helix, as contrasted with that of the competing alpha-helical structure, is explicitly incorporated into a theoretical model for the 3(10)-helix/alpha-helix equilibrium constant for a given peptide. Finite length effects and the "extra" intrahelical hydrogen bond of the 3(10) form are expressed naturally as a result of this loop analysis. This semiempirical model captures all the established features of existing empirical rules for helical conformational transitions in Aib-rich sequences, as well as the recently detected helical transition induced solely by sequence permutation.
40 citations