• No results found

Dynamics in electron transfer protein complexes Bashir, Q.

N/A
N/A
Protected

Academic year: 2021

Share "Dynamics in electron transfer protein complexes Bashir, Q."

Copied!
3
0
0

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

Hele tekst

(1)

Dynamics in electron transfer protein complexes

Bashir, Q.

Citation

Bashir, Q. (2010, October 27). Dynamics in electron transfer protein complexes. Retrieved from https://hdl.handle.net/1887/16077

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/1887/16077

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

(2)

Acknowledgements

175

Acknowledgements

First of all I am grateful to Prof. Dr. Marcellus Ubbink for providing me the opportunity to start PhD research at Leiden University and his esteemed guidance during the four years of research.

I am thankful to the Higher Education Commission (HEC) of Pakistan for providing me the PhD scholarship. I would like to thank the Netherlands Organization for International Cooperation in Higher Education (NUFFIC) for managing my scholarship and insurance matters. I would also like to acknowledge Leiden University for providing me partial funding for the last three years of my PhD.

I am thankful to the collaborators: Prof. Dr. Matthias Ullmann for providing the program for simulations and the related technical help, Prof. Dr. W.J.H. van Berkel and Dr. N.G.H. Leferink for providing some protein samples.

Dr. Alexander N. Volkov is acknowledged for his support during the initial stages of my PhD. Thanks to Dr. Francesco Scarpelli for the EPR measurements.

I would like to thank Elisabeth Meulenbroek and Dr. Navraj Pannu for their help in crystallization and solving the crystal structures of protein complexes.

I am grateful to Bharat Somireddy, Dipen Shah and Ruta Nachane for their wonderful company, outings and discussions.

I would like to acknowledge Dr. Peter Keizers for the Dutch translation of the summary and for his help at multiple occasions during my PhD. I am also thankful to Dr. Xinfu Xu, Dr. Rinske Hulsker, Dr. Hanna Lindfors, Dr. Matthias Hass as well as Simon Skinner, Sandra Scanu, Yoshitaka Hiruma, Wei-Min Liu and Jia-Ying Guan for general and scientific discussions. I am thankful to Anneloes Blok and Lionel Ndamba for their lab support. Thanks to all other members of the Protein Chemistry group for providing a wonderful research environment.

Kees Erkelens, Fons Lefeber and Karthick Babu are acknowledged for maintaining the NMR facility and the related technical help. Thanks to Roelf van der Kleij for his technical help related to Linux.

I would like to thank Dr. Muhammad Jahangir for introducing me to EndNote and helping me in thesis formatting. I am thankful to Dr. Soban Umar, Dr. Farrakh Mehboob, Dr. Ghulam Hasnain, Aamir Aziz, Muhammad Tariq, Muhammad Shahbaz

(3)

Acknowledgements

176

Anwar, Asghar Ali, Kashif Ali and other Pakistani and non-Pakistani friends for providing me great company, support and suggestions at different occasions.

I would like to acknowledge all my teachers in my academic career. I am especially indebted to Prof. Dr. Naeem Rashid for all encouragement, support and guidance which put me on the path of a scientific career.

Special thanks to my brothers and sisters for sharing happiness and providing me support and guidance in all moments of my life. Finally, I would like to express my profound gratitude to my parents for their love, support and trust.

Referenties

GERELATEERDE DOCUMENTEN

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

calculated for combinations of PREs from the specific structure and the simulated ensemble at different population fractions of the encounter complex (p, eq

A vast body of literature investigating the impact of interfacial mutations on protein-protein association reactions addresses the equilibrium between the free and bound forms,

In the small electron transfer complexes, most of the orientations in the encounter complex bring the redox centers within the required distance and thus the role of the

The structures using two different sets of spin label orientations differ from each other with rms deviation of 2.8 Å and from the crystal structure with rms deviation of 3.5 Å

The concentrated protein solution is then applied to G-75 gel-filtration column equilibrated with 20 mM NaPi pH 6.0 containing 100 mM NaCl and eluted with the equilibration buffer..