• No results found

Approaches to structure and dynamics of biological systems by electron-paramagnetic-resonance spectroscopy Scarpelli, F.

N/A
N/A
Protected

Academic year: 2022

Share "Approaches to structure and dynamics of biological systems by electron-paramagnetic-resonance spectroscopy Scarpelli, F."

Copied!
7
0
0

Bezig met laden.... (Bekijk nu de volledige tekst)

Hele tekst

(1)

Approaches to structure and dynamics of biological

systems by electron-paramagnetic-resonance spectroscopy

Scarpelli, F.

Citation

Scarpelli, F. (2009, October 28). Approaches to structure and dynamics of biological systems by electron-paramagnetic-resonance spectroscopy.

Casimir PhD Series. Retrieved from https://hdl.handle.net/1887/14261

Version: Corrected Publisher’s Version

License: Licence agreement concerning inclusion of doctoral thesis in the Institutional Repository of the University of Leiden

Downloaded from: https://hdl.handle.net/1887/14261

Note: To cite this publication please use the final published version (if applicable).

(2)

List of Publications

Scarpelli F., Guzzi R., Bartucci R., Sportelli L. – Pulsed EPR Study of Spin Labeled Hemoglobin – to be submitted.

Scarpelli F., Drescher M., Meijneke T., Holt A., Rijkers D., Killian J.A., Huber M. – Aggregation of Transmembrane Peptides Studied by Spin- Label EPR – Journal of Physical Chemistry B, submitted.

Milikisyants S., Scarpelli F., Finiguerra M., Ubbink M., Huber M.,– A pulsed EPR method to determine distances between paramagnetic centers with strong spectral anisotropy and radicals: The dead-time free RIDME sequence – Journal of Magnetic Resonance, submitted

Scarpelli F., Gast P., Milikisyants S., Murphy M.E.P., Arrieta A.L., Groenen E.J.J., Huber M. – A 95 GHz single crystal EPR study of the type 2 copper site of the M150E mutant of the nitrite reductase of Alcaligenes faecalis – in preparation

Scarpelli F., Volkov A., Bashir Q., Ubbink M., Huber M., – Dynamics of spin labels at surface sites of cytochrome c peroxidase by EPR– in preparation

(3)
(4)

Curriculum Vitae

of Francesco Scarpelli, born in Cosenza (Italy), on April 3, 1976.

In 1996, after I received the diploma from Liceo Scientifico G. B. Scorza in Cosenza, I joined the Department of Physics at the Università degli studi della Calabria. I spent the last two and a half years of my studies working on my graduation thesis in the group of Prof. L. Sportelli at the Department of Molecular Biophysics. My thesis project concerned the study of a spin-labeled hemoglobin by pulsed EPR. In July 2004, I graduated in Physics, with a specialization in Molecular Biophysics, at the Università degli studi della Calabria.

In March 2005, I started a PhD project at the Department of Molecular Physics of Leiden University, under the supervision of dr. M. Huber and prof. dr. E.J.J. Groenen. In this research project, I was involved in methodological developments and the application of EPR in the study of dynamics and structure of systems that involve transition metal ions and nitroxide spin labels. During my PhD I assisted in the physics courses for 1st and 3rd year biology students. In July 2005, I attended the

“Advanced EPR methods in Biophysics” school in Wiesbaden (Germany). In March 2006, I followed the “EasySpin, spectral simulation and data analysis in EPR spectroscopy” school at the ETH in Zurich. I have presented the results of my research at the 16th Benelux EPR society meeting (May 2008, Gent) and the “Advanced Paramagnetic Resonance in Molecular Biophysics” meeting (September 2008, Siena).

(5)
(6)

Nawoord

The last four years have been a great experience on both professional and personal level. During my PhD I had the opportunity to meet a lot of interesting people without whom this thesis would not be written now.

First of all I would like to thank dr. Sergey Milikisyants, he has been a guide during this “journey” and also a good friend. Almost all I know about EPR is thank to him.

I am also grateful to dr. Martina Huber for the patience and the precious help in the realization of this thesis and dr. prof. Edgar Groenen for the useful and interesting discussions and suggestions.

A special thanks to Peter Gast, for his help and patience during long and frustrating measurements and Malte Drescher for the useful discussions and collaboration in one of my project.

Thank to Alex Volkov and Qamar Bashir for the spin labelled cytocrhome and Marcellus Hubbink for the useful help.

I owe Michael Murphy and Angela Arrieta my gratitude for the NiR proteins and crystals.

A big thank to the whole MoNOS group, I can not image a better and more friendly environment where I could do my PhD. A particular thanks to Jennifer Mathies for the help in the final step of the thesis and the funny discussions and Michael Galouzis, the best office mate I could have; I have had a very nice time with him and shared a lot of common interests.

A very special thanks to Anna Pezzarossa for the fantastic time we spent, for the always interesting discussions and for being there always when I needed help and support.

I want to mention also some important people that have been and always will be part of my life, my appreciation goes to Francesco, Carmine, Emilio and Loredana.

(7)

Referenties

GERELATEERDE DOCUMENTEN

License: Licence agreement concerning inclusion of doctoral thesis in the Institutional Repository of the University of Leiden Downloaded.

Chapter 4 Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c

Free proteins (A) associate to form encounter complex (B) consisting of multiple protein orientations which leads to the formation of single orientation specific complex

The residues of yeast Cc showing the highest chemical shift perturbations (> 0.25 ppm) are conserved among both Arabidopsis Cc paralogs, including Thr12 (Figure 2.4),

137 and our preset data, we would like to propose that binding energy hot spots, which are prevalent in static protein complexes, 129,132,135 can also govern transient

broadening of the Fe(III) signal.. The longitudinal relaxation rate is related to the saturation factor 3 Z. From the power P the value of H 1 can be calculated according to Eq.

In the last decade several pulsed EPR methods have been developed and used to measure distances and to determine the structure of chemical and biological systems from the

The rotation-correlation times of spin labels at different surface sites of proteins provide a better ranking of the spin-label mobility than the lineshape