Postdoctoral Research Associate - Chemical Biology & Therapeutics

Job Location US-TN-Memphis
Chemical Biology & Therapeutics
Faculty Member
Marcus Fischer


Postdoc project in dynamic structural biology:

Exploiting Water Network Perturbations in Protein Binding Sites

We are recruiting a postdoc for a structural biology project that investigates the role of water networks at protein ligand interfaces with a view towards ligand discovery. The position is available immediately and NIH funded for 4 years.

We are looking for highly motivated candidates with curiosity and skills to reveal hidden factors that contribute to protein-ligand binding and leverage this information for ligand discovery. As this project integrates experimental and computational data it will require both a solid background in structural biology and significant computational skills for custom data analysis and automation. Despite the focus on computational structural biology, we will consider exceptional candidates with a suitable experimental background and a strong interest in protein dynamics, ligands and water.

The project is housed in the Department of Chemical Biology and Therapeutics, and Structural Biology at St. Jude Children’s Research Hospital. It builds on strong investments into a world-class infrastructure in structural and chemical biology. You will be embedded into a dynamic lab that has strong expertise in modulating protein conformational ensembles with ligands and temperature (see references below). This is an exciting time to join us and build a career while living in an affordable city.


Please direct your questions and application package including a cover letter, current CV, and 3 letters of reference to: Dr. Marcus Fischer (

Relevant papers include:
• Bradford et al. (2021). Temperature artifacts in protein structures bias ligand-binding predictions. Chemical Science.
DOI: 10.1039/D1SC02751D
• Fischer (2021). Macromolecular room temperature crystallography. Q Rev Biophys 54. E1
• Darby et al. (2019). Water Networks Can Determine the Affinity of Ligand Binding to Proteins. JACS 141, 15818-26.
• Balius et al. (2017). Testing inhomogeneous solvation theory in structure-based ligand discovery. PNAS E6839-46.
• Fischer et al. (2015). One crystal, two temperatures: cryocooling penalties alter ligand binding to transient protein sites.
Chembiochem 1560-64.
• Fischer et al. (2014). Incorporation of protein flexibility & conformational energy penalties in docking screens to improve ligand
discovery. Nature Chemistry 6, 575-83.

More info at:

Minimum Experience

- PhD in structural biology or related field
- High proficiency in coding including Python
- Interest in dynamic aspects of structural biology including protein flexibility and hydration


Optional requirements:
- Hands-on experience in molecular biology, crystallography, xFEL, biophysical assays
- Molecular dynamics, free-energy perturbation, ligand discovery, computational chemistry

Other Information

St. Jude is an Equal Opportunity Employer

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COVID-19 vaccine:

St. Jude Children’s Research Hospital has mandated the COVID-19 vaccine for all employees, excluding those with an approved medical or religious accommodation, as a condition of employment.


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