Integrated Computational Approach to the Electron Paramagnetic Resonance Characterization of Rigid 310-Helical Peptides with TOAC Nitroxide Spin Labels | Zendy

Marco Gerolin | Zendy; Mirco Zerbetto | Zendy; Alessandro Moretto | Zendy; Fernando Formaggio | Zendy; Claudio Toniolo | Zendy; Martin van Son | Zendy; Maryam Hashemi Shabestari | Zendy; Martina Huber | Zendy; Paolo Calligari | Zendy; Antonino Polimeno | Zendy

Open Access

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) - electron paramagnetic resonance , nitroxide mediated radical polymerization , characterization (materials science) , spin (aerodynamics) , site directed spin labeling , spin label , nuclear magnetic resonance , electron , paramagnetism , resonance (particle physics) , materials science , molecular physics , chemistry , condensed matter physics , physics , atomic physics , nanotechnology , quantum mechanics , polymer , radical polymerization , copolymer , thermodynamics

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.

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