Solvent effect on librational dynamics of spin-labelled haemoglobin by ED- and CW-EPR
作者： Francesco Scarpelli , Rosa Bartucci , Luigi Sportelli , Rita Guzzi
DOI: 10.1007/S00249-010-0644-5
关键词: Chemistry 、 Hyperfine structure 、 Spectral line 、 Spin label 、 Analytical chemistry 、 Protein dynamics 、 Solvent 、 Solvent effects 、 Nitroxide mediated radical polymerization 、 Electron paramagnetic resonance 、 Biophysics 、 General Medicine
摘要: Two-pulse, echo-detected electron paramagnetic resonance (ED-EPR) spectra and continuous-wave EPR (CW-EPR) were used to investigate the solvent effect on librational motion of human haemoglobin spin-labelled cysteine β93 with nitroxide derivative maleimide, 6-MSL. Protein samples fully hydrated in phosphate buffer solution (PBS), a 60% v/v glycerol/water mixture lyophilized form measured at cryogenic temperature frozen state. The protein was characterized by amplitude-correlation time product, τ(c), deduced from ED-EPR spectra. amplitude, determined independently, motionally averaged hyperfine splitting CW-EPR spectra, correlation time, derived combination pulsed conventional data. Rapid small amplitude detected all samples. In each case, dynamics restricted up 180 K, beyond which it increased steeply for PBS presence glycerol. contrast, dehydrated protein, hindered less dependent ~240 K. samples, deviated values only T > 200 where rapid increase evident whereas limited variation shown sub-nanosecond regime weakly temperature. results evidence that favours dynamics.
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