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The complete chirospectroscopic signature of the peptide 310-helix in aqueous solution

✍ Scribed by Claudio Toniolo; Fernando Formaggio; Sabrina Tognon; Quirinus B. Broxterman; Bernard Kaptein; Rong Huang; Vladimir Setnicka; Timothy A. Keiderling; Iain H. McColl; Lutz Hecht; Laurence D. Barron


Book ID
101719271
Publisher
Wiley (John Wiley & Sons)
Year
2004
Tongue
English
Weight
242 KB
Volume
75
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

We synthesized by solution methods a water‐soluble, terminally blocked heptapeptide based on five markedly helicogenic, C^α^‐tetrasubstituted α‐amino acids C^α^‐methyl‐L‐norvalines and two strongly hydrophilic 2‐amino‐3‐[1‐(1,4,7‐triazacyclononane)]‐L‐propanoic acid residues at positions 2 and 5. A Fourier transform infrared absorption and NMR analysis in deuterated chloroform and aqueous solutions of the heptapeptide and two side‐chain protected synthetic precursors confirmed our working hypothesis that all oligomers are folded in the 3~10~‐helical conformation. Based on these findings, we exploited this heptapeptide as a chiral reference compound for detailed electronic CD, vibrational CD, and Raman optical activity characterizations of the 3~10~‐helix in aqueous solution. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004


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