
Integrated Computational Approach to the Electron Paramagnetic Resonance Characterization of Rigid 310-Helical Peptides with TOAC Nitroxide Spin Labels
Author(s) -
Marco Gerolin,
Mirco Zerbetto,
Alessandro Moretto,
Fernando Formaggio,
Claudio Toniolo,
Martin van Son,
Maryam Hashemi Shabestari,
Martina Huber,
Paolo Calligari,
Antonino Polimeno
Publication year - 2017
Publication title -
the journal of physical chemistry. b
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 392
eISSN - 1520-6106
pISSN - 1520-5207
DOI - 10.1021/acs.jpcb.7b01050
Subject(s) - nitroxide mediated radical polymerization , electron paramagnetic resonance , spin label , chemistry , stereochemistry , amino acid , molecule , peptide , crystallography , nuclear magnetic resonance , organic chemistry , biochemistry , physics , radical polymerization , copolymer , polymer
We address the interpretation, via an integrated computational approach, of the experimental continuous-wave electron paramagnetic resonance (cw-EPR) spectra of a complete set of conformationally highly restricted, stable 3 10 -helical peptides from hexa- to nonamers, each bis-labeled with nitroxide radical-containing TOAC (4-amino-1-oxyl-2,2,6,6-tetramethylpiperidine-4-carboxylic acid) residues. The usefulness of TOAC for this type of analysis has been shown already to be due to its cyclic piperidine side chain, which is rigidly connected to the peptide backbone α-carbon. The TOAC α-amino acids are separated by two, three, four, and five intervening residues. This set of compounds has allowed us to modulate both the radical···radical distance and the relative orientation parameters. To further validate our conclusion, a comparative analysis has been carried out on three singly TOAC-labeled peptides of similar main-chain length.