Welcome to Protein Chemistry
Protein Chemistry March 2014

Protein Chemistry is a section of the Leiden Institute of Chemistry at Leiden University. The section is headed by Prof. Dr. Marcellus Ubbink.

The research is aimed at understanding protein & nucleic acid structure, function and interactions. Particular interests comprise protein-protein interactions & enzyme function (Prof. Ubbink) and chromatine research, such as structure and function of nucleosomes (Dr. van Ingen) and biophysical aspects of protein - DNA interactions (Dr. Dame).

The section houses equipment for recombinant protein production and a variety biophysical characterisation methods.


Remus Dame joins Protein Chemistry group

Dr Remus Dame and his coworkers have joined Protein Chemistry, expanding our research in protein - DNA interactions. Dr Dame uses in vitro and in cell techniques to study how proteins influence the physical and functional properties of DNA.

The website will be updated soon to accommodate the new research lines of Dr Dame and Dr van Ingen (see news item December 2, 2014).

KIEM project awarded

NWO has awarded a KIEM project to Prof. Marcellus Ubbink.

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Hugo van Ingen new assistant professor in Protein Chemistry

The Leiden Institute of Chemistry and the section of Protein Chemistry welcome Hugo van Ingen as a staff member. Van Ingen is appointed as tenure-track assistant professor and will set up his new research group focusing on the molecular basis of chromatin function.

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Science in Transition

Prof. Frank Miedema, a leading person in the new movement called Science in Transition, will speak in the Gorlaeus Laboratories on March 24, 2014 at 15:30 in lecture theatre C1.

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ECHO grant for Marcellus Ubbink

An ECHO grant has been awarded to Marcellus Ubbink for research in dynamic protein complexes. The project is aimed at manipulating a protein interface to change the encounter state of the complex. This state is the essential prelude to forming an active protein-protein complex. The project will elucidate how important electrostatic interactions are for homing in on the final binding site.