Germany : PhD Scholarships-NRW Research School BioStruct

The NRW Research School BioStruct – Biological Structures in Molecular Medicine and Biotechnology at Heinrich-Heine-University Düsseldorf in Germany, funded by the Ministry of Innovation, Science, Research and Technology of the German Federal State North Rhine-Westphalia (NRW), and the school chairmen Prof. Dr. Lutz Schmitt and Prof. Dr. Dieter Willbold invite applications on PhD Scholarships starting in Spring 2012.

BioStruct offers innovative PhD education and research programs within a stimulating interdisciplinary environment combining the field of structural biology with molecular medicine and biotechnology. Highly motivated and excellent candidates holding an MSc or Diploma degree in the fields of Biochemistry, Biology, Chemistry, Physics and related fields can directly apply for a PhD Scholarship for the project "Structure of the nisin resistance protein”

including a monthly stipend of 1345,- EUR and contributions towards travel and research expenses.

Candidates should have a strong background in protein biochemistry, especially protein expression and purification. Furthermore, an interest in x-ray crystallography is a prerequisite. Workplace will be the “Heinrich-Heine-University” in the group of Prof. Dr. Lutz Schmitt: Dr. Sander Smit’s Group.


PhD Research Project Summary: Lantibiotics are antimicrobial peptides produced by Gram-positive bacteria acting against other Gram-positive bacteria found in the habitat. The best studied lanthibiotic is nisin, which is a 34 amino acid long peptide which comprises five (methyl) lanthionine rings produced by Lactococcus lactis. The potency of nisin to penetrate the membrane and inducing lysis of the target organism is extremely high since only a few nisin molecules are required to induce cell lysis. In contrast to nisin producer strains, the target
organisms developed a defense mechanism consisting of the nisin resistance protein (NSR). In vitro studies demonstrated the capability of NSR to cleave nisin between MeLan28 and Ser29. The obtained nisin fragment, which still contains the five characteristic lanthionine rings, is 100 fold less active compared to full-length nisin. The NSR family is the first example for resistance against nisin, although the latter has been used in (food) industry already for several decades.

The goal of this PhD project is to elucidate the structure of NSR with and without bound substrate as well as to identify the molecular mechanism of substrate recognition and cleavage. Techniques used during this protein will include molecular biology, protein biochemistry and purification, fluorescence spectroscopy and X-ray crystallography

For further information on the NRW Research School BioStruct, prerequisites and mandatory application forms please visit our website:

Further Information

Application Deadline : 20 February 2012

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Posted on 2012-01-26 04:28:20

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