Postdoctoral Fellow
- University of Maryland
- Location: Rockville, MD
- Job Number: 7106960
- Posting Date: Aug 1, 2022
- Application Deadline: Open Until Filled
Job Description
Postdoctoral Positions in Structural Biology
Two NIH-funded postdoctoral positions in protein crystallography available at the University of Maryland Institute for Bioscience and Biotechnology Research (IBBR) for recent PhDs to join a multidisciplinary team investigating the structural basis for pathogen and tumor cell recognition by the human immune system. Several classes of recognition molecules are under study: antibodies, T cell receptors (TCRs), and natural killer (NK) cell receptors. Projects include X-ray crystallographic and cryoEM studies of: 1) tumor-specific and SARS-CoV-2-specific TCRs, 2) NK receptor recognition of cellular and viral ligands, 3) TCR–CD3 complex, 4) structure-based design of hepatitis C vaccine, and 5) structure-based design of small molecule antiviral drugs. Experience in molecular biology and recombinant protein expression is highly desirable. [Nat. Commun. 11, 2908 (2020); J. Mol. Biol. 432, 166697 (2020); PNAS 118, e2015149118 (2021); J. Mol. Biol. 433, 166714 (2021); J. Med. Chem. 64, 18010 (2021); Biochemistry 61, 822 (2022); PNAS 119, e2112008119 (2022); Nat. Commun. 13, 19 (2022)]. Visit http://www.ibbr.umd.edu/profiles/roy-mariuzza. State-of-the-art X-ray, cryoEM, and NMR facilities. Excellent opportunities for collaborative studies in cryoEM and NMR. IBBR, a joint research center of the University of Maryland and the National Institute of Standards and Technology (NIST), is located in the heart of a major biotech community that includes AstraZeneca and GlaxoSmithKline. Send CV and names of three references to Dr. Roy A. Mariuzza ([email protected]).
The University of Maryland is an Equal Opportunity Employer.
Two NIH-funded postdoctoral positions in protein crystallography available at the University of Maryland Institute for Bioscience and Biotechnology Research (IBBR) for recent PhDs to join a multidisciplinary team investigating the structural basis for pathogen and tumor cell recognition by the human immune system. Several classes of recognition molecules are under study: antibodies, T cell receptors (TCRs), and natural killer (NK) cell receptors. Projects include X-ray crystallographic and cryoEM studies of: 1) tumor-specific and SARS-CoV-2-specific TCRs, 2) NK receptor recognition of cellular and viral ligands, 3) TCR–CD3 complex, 4) structure-based design of hepatitis C vaccine, and 5) structure-based design of small molecule antiviral drugs. Experience in molecular biology and recombinant protein expression is highly desirable. [Nat. Commun. 11, 2908 (2020); J. Mol. Biol. 432, 166697 (2020); PNAS 118, e2015149118 (2021); J. Mol. Biol. 433, 166714 (2021); J. Med. Chem. 64, 18010 (2021); Biochemistry 61, 822 (2022); PNAS 119, e2112008119 (2022); Nat. Commun. 13, 19 (2022)]. Visit http://www.ibbr.umd.edu/profiles/roy-mariuzza. State-of-the-art X-ray, cryoEM, and NMR facilities. Excellent opportunities for collaborative studies in cryoEM and NMR. IBBR, a joint research center of the University of Maryland and the National Institute of Standards and Technology (NIST), is located in the heart of a major biotech community that includes AstraZeneca and GlaxoSmithKline. Send CV and names of three references to Dr. Roy A. Mariuzza ([email protected]).
The University of Maryland is an Equal Opportunity Employer.
