Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5169
Title: Molecular motion of spin labeled side chains in the C-terminal domain of RGL2 protein: a SDSL-EPR and MD study
Authors: S., Pistolesi
Ferro, ELISA MARIA PAOLA
Santucci, Annalisa 
Basosi, Riccardo 
Trabalzini, Lorenza 
Pogni, Rebecca 
Issue Date: 2006
Project: None 
Journal: BIOPHYSICAL CHEMISTRY
Abstract: 
Five singly spin labeled side chains at surface sites in the C-terminal domain of RGL2 protein have been analyzed to investigate the general relationship between nitroxide side chain mobility and protein structure. At these sites, the structural perturbation produced by replacement of a native residue with a nitroxide side chain appears to be very slight at the level of the backbone fold. The primary determinants of the nitroxide side chain mobility are backbone dynamics and tertiary interactions. On the exposed surfaces of alpha-helices, the side chain mobility is not restricted by tertiary interactions but appears to be determined by backbone dynamics, while in loop sites, the side chain mobility is even higher. For a better understanding of the changes in the EPR spectral line shape, molecular dynamics simulations were performed and found in agreement with EPR spectral data.
Description: 
38207
URI: http://hdl.handle.net/20.500.12779/5169
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2006.03.021
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