New Fourier transform infrared based computational method for peptide secondary structure determination. II. Application to study of peptide fragments reproducing processing site of ocytocin–neurophysin precursor

✍ Scribed by Mario Simonetti; Carlo Di Bello

• Publisher: Wiley (John Wiley & Sons)
• Year: 2001
• Tongue: English
• Weight: 422 KB
• Volume: 62
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1003

✦ Synopsis

Abstract

A new method for the quantitative determination of the percentage of intramolecular H‐bonds, based on Fourier transform infrared techniques, is applied to the conformational analysis of a series of synthetic peptides spanning the processing site of the ocytocin and neurophysin precursor. Even though the method uses traditional tools such as Fourier self‐deconvolution, the __N__th derivative, and curve‐fitting procedures for the analysis of the spectra, the assignment of the absorptions due to peptide groups participating into secondary structures is based on the direct observation and quantification of the isotopic effect induced on the groups participating in intramolecular H‐bonds in the presence of organic solvents. This permits the quantification of the different populations of molecules containing intramolecular H‐bonds involved in β‐turns and α‐helices. The results are consistent with those previously obtained by NMR techniques in the same solvent systems. © 2001 John Wiley & Sons, Inc. Biopolymers (Biospectroscopy) 62: 109–121, 2001