𝔖 Bobbio Scriptorium
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Sensitive Criteria for the Critical Size for Helix Formation in Oligopeptides

✍ Scribed by Murray Goodman, Antonio S. Verdini, Claudio Toniolo, William D. Phillips and Frank A. Bovey

Book ID
123649405
Publisher
National Academy of Sciences
Year
1969
Tongue
English
Weight
306 KB
Volume
64
Category
Article
ISSN
0027-8424

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## Abstract The circular dichroism of a series of L‐methionine oligopeptides [BOC‐(Met)~__n__~‐OMe] was examined in trifluoroethanol and hexafluoroacetone sesquihydrate. The results indicate that the trimer through the hexamer exists predominantly in disordered conformations in these solvents. An a

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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 a-mono-alkylated residues. The distinct hydrogen-bonding network of the 310helix, as contrasted with that of