Post-doctoral fellowship in biochemistry/glycobiology – M/F

Cnrs Inc; France; On-site; EUR 42,000 - 66,000; Full time

Job summary

CNRS Institute of Structural Biology in Grenoble invites applications for a temporary researcher position focusing on glycosaminoglycan-targeting sulfatases. The role involves engineering enzymes, characterizing mutants, and reporting results at conferences.

Join the SAGAG group to advance structural biology, enzymology and glycan biology within a vibrant international research environment, located in Grenoble Science Park.

Qualifications

• Expertise in recombinant protein production.
• Expertise in enzymology.
• In-depth knowledge of structural biology.
• In-depth knowledge of glycosaminoglycan (GAG) biology.
• English (written/oral) level B2 minimum.

Responsibilities

• Study the structure and functional properties of a bacterial sulfatase targeting glycosaminoglycans.
• Express and purify recombinant enzymes.
• Perform enzymatic activity assays and determine kinetic parameters.
• Develop protein design approaches to generate mutants with improved enzymatic properties.
• Validate the enzymatic properties of selected mutants.
• Determine the structures of selected mutants using X-ray crystallography.
• Present research findings at scientific congresses and conferences.
• Write activity reports and scientific publications.

Skills

recombinant protein production

enzymology

glycosaminoglycan biology

structural biology

Job description

Biological sciences » Biological engineering

Organisation/Company CNRS Department Institut de biologie structurale Research Field Chemistry Physics » Biophysics Biological sciences » Biological engineering Researcher Profile Established Researcher (R3) Application Deadline 26 Nov 2026 - 23:59 (UTC) Country France Type of Contract Temporary Job Status Full-time Hours Per Week 35 Offer Starting Date 1 Jan 2027 Is the job funded through the EU Research Framework Programme? Not funded by a EU programme Is the Job related to staff position within a Research Infrastructure? No

Offer Description

Study the structure and functional properties of a bacterial sulfatase targeting glycosaminoglycans. Generate and characterize mutants aimed at improving the enzyme's properties.

• Express and purify recombinant enzymes.
• Perform enzymatic activity assays and determine kinetic parameters.
• Develop protein design approaches to generate mutants with improved enzymatic properties.
• Validate the enzymatic properties of selected mutants.
• Determine the structures of selected mutants using X-ray crystallography.
• Present research findings at scientific congresses and conferences.
• Write activity reports and scientific publications.

Located on the Grenoble Science Park (ESRF/ILL/EMBL/IBS), the Institute of Structural Biology (IBS) is a national and international player in the field of integrated structural biology. The IBS is a research center, a technical platform, a host site and a scientific training center. Its mission is to develop research in structural biology, a field of research that is crucial to the understanding of fundamental biological mechanisms. It is supported by 12 state-of-the-art platforms.
As a joint research unit (CEA-CNRS-UGA), the IBS is composed of 20 research groups, each of which proposes a multi-disciplinary approach, at the frontiers of biology, physics and chemistry, in coherence with 3 research axes. Nearly 320 people work there as researchers, PhD students, engineers and technicians in a multicultural and international environment.
The person recruited will join the SAGAG group working on glycosaminoglycans ( https://www.ibs.fr/en/research/membrane-proteins-and-glycobiology/struc… ).

Research Field Biological sciences » Biological engineering Years of Research Experience 4 - 10

Additional Information

Eligibility criteria

• Expertise in recombinant protein production.
• Expertise in enzymology.
• In-depth knowledge of structural biology.
• In-depth knowledge of glycosaminoglycan (GAG) biology.
• English (written/oral) level B2 minimum