We are recruiting a postdoc for a computational 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 5 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. The project is embedded into a dynamic lab that has strong expertise in modulating protein conformational ensembles with ligands and temperature (see references below). The project is housed in the Department of Chemical Biology and Therapeutics <https://www.stjude.org/research/departments-divisions/chemical-biology-therapeutics.html>, and Structural Biology <https://www.stjude.org/research/departments-divisions/structural-biology.html> at St. Jude Children’s Research Hospital. It builds on strong investments into a world-class infrastructure in structural and chemical biology. This is an exciting time to join us and build a career while living in an affordable city. This postdoc position is NIH funded for 5 years. Please direct your questions and application package including a cover letter, current CV, and 3 letters of reference to: Dr. Marcus Fischer ( marcus.fisc...@stjude.org). 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: https://www.stjude.org/fischer Minimum Education - PhD in structural biology or related field Minimum Experience - High proficiency in coding incl Python - Interest in dynamic aspects of structural biology including protein flexibility and hydration Optional requirements: - Hands-on molecular biology and crystallography experience https://postdoc-stjude.icims.com/jobs/8641/postdoctoral-research-assoc/job ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
