Job opportunity

Publication date:

Oct 21st 2019

Two Post-doctoral and two PhD Vacancies in Heck-lab

 

 In the Heck-lab at Utrecht University (www.hecklab.com) a variety of exciting research projects seek motivated researchers to tackle them. The research emphasis is on the development of advanced mass spectrometry-based methods to address questions in proteomics and structural biology. The Heck-lab houses and excellent infrastructure, including a dozen state-of-the-art mass spectrometers, advanced separation technologies, bioinformatics and laboratories for cell culture, biochemistry and molecular biology. The research group is quite vibrant with over 15 nationalities being present. Utrecht is a great place to be.

PhD Positions (4 year program)

 

1. Personalized profiling of patient serum autoantibodies by de novo sequencing

Characterization and de novo sequencing of endogenous antibodies, with the aim to pick up antibodies raised by our immune system against rheumatoid arthritis. In this project you will develop and apply methods for the profiling and in-depth characterization of the variable domain of (auto)antibodies using native, top-down and middle-down mass spectrometry approaches, leading to the personalized profiling of patient serum autoantibodies linked to rheumatoid arthritis. You have ideally a background in pharmaceutical sciences, biomedical sciences and/or analytical chemistry.

 

2. Mass Spectrometry and Chemical Proteomics

Detailed characterization and of protein-drug interactions to identify targets and undesired off-targets of drugs. Novel chemical biology approaches will be combined with affinity enrichment and mass spectrometry. Several drug molecules will be targeted, among them anti-cancer drugs. You have ideally a background in pharmaceutical sciences and/or analytical biochemistry.

Postdoc positions (minimum of 2 years)

 

1. Viruses and other macromolecular assemblies studied by Biomolecular Mass Spectrometry

You will focus on the further optimization of native mass spectrometry and top-down proteomics for the analysis of macromolecular complexes, notably viruses, with the aim to generate even higher sensitivity and resolving power, contributing to the further development of single particle charge detection mass spectrometry. As some viruses are used for gene-delivery this project will partly be in collaboration with industry. You have ideally a background in biophysical and/or analytical chemistry.

 

2. Monitoring and Visualizing Protein Societal Behavior in the Cell; an Integrative Approach

The main goal is to develop an integrated approach to characterize proteins and their assemblies in the thermophiles Pyrococcus furiosusand Thermus thermophilus. Both these organisms are evolutionary fascinating and perfectly amendable as model systems in integrated structural biology. You will be part of a consortium that will use a combination of analytical and biophysical techniques with integrative structural modelling strategies. You will focus on native MS, top-down proteomics and crosslinking mass spectrometry (XL-MS) to uncover protein complexes in an unbiased fashion, ideally in their native state and ultimately in situ. You have ideally a background in biophysical and/or analytical chemistry.

Information

  • Position: PhD and PostDoc
  • Location: Utrecht University, Utrecht, Netherlands
  • Duration: 4 years (PhD) and 2 years (PostDoc)
  • Startdate: After consultation
  • Background: Experience with Proteomics Workflows, systems biology, high end proteomics  is appreciated
  • Apply with motivation letter, cv and 2 references
  • Deadline for application: 30 Nov 2019
  • For information or application: c.c.heuzer@nulluu.nl

 

Recent illustrative work of Heck-lab

  • Potel CM, Lin MH, Heck AJR & Lemeer S (2018) Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics Nature Methods. 15:187-190.
  • van de Waterbeemd M, et al. (2018) Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods Nature Communications 9:2493.
  • Snijder J, et al. (2017) Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science. 355:1181-1184.
  • Liepe J, et al. (2016) A large fraction of HLA class I ligands are proteasome-generated spliced peptides. Science. 354:354-358.
  • Liu F, Rijkers DT, Post H, Heck AJ. (2015) Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry. Nature Methods. 12:1179-84.