Post Doctoral Fellow (NCI) - Frederick, MD | Biospace
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Post Doctoral Fellow (NCI)

Leidos Biomedical Research, Inc.

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Location:
Frederick, MD
Posted Date:
10/31/2016
Position Type:
Full time
Job Code:
632630
Salary:
Required Education:
Doctorate/PhD
Areas of Expertise Desired:
Structural Biology,

Job Description

COMPANY INFORMATION
Leidos Biomedical Research, Inc. (LBRI), a wholly owned subsidiary of Leidos, operates the Frederick National Laboratory for Cancer Research (FNLCR). FNLCR is a Federally Funded Research and Development Center (FFRDC) sponsored by the National Cancer Institute (NCI). It is the only FFRDC dedicated to biomedical research. Through its status as an FFRDC, FNLCR provides NCI and others with a unique national resource to accelerate the development and delivery of effective preventive, diagnostic, and therapeutic products for cancer and AIDS.

The breadth of FNLCR’s activities spans the research and development spectrum, including investigator-initiated, hypothesis-driven research into cancer and AIDS; advanced technology programs focused on genetics and genomics, proteins and proteomics, imaging, nanotechnology, bioinformatics, and laboratory animal sciences; clinical operations in support of NCI and National Institute of Allergy and Infectious Diseases (NIAID)-sponsored clinical trials, as well as NCI drug discovery and development efforts; and management and operations of biopharmaceutical development and manufacturing programs under current Good Manufacturing Practice conditions for NCI and NIAID. Administrative, procurement, financial, safety, and facilities support is provided to these R&D activities through state-of-the-art business processes.  LBRI has approximately 1,900 employees and manages an annual operating budget of approximately $450M.

For more information about Leidos Biomedical Research Inc., please visit our webpage at http://www.leidosbiomed.com/

PROGRAM DESCRIPTION
The Basic Science Program (BSP) pursues independent, multidisciplinary research programs in basic or applied molecular biology, immunology, retrovirology, cancer biology or human genetics.  Research efforts and support are an integral part of the Center for Cancer Research (CCR) at the Frederick National Laboratory for Cancer Research (FNLCR).

As part of the BSP, the Structural Biology section of the Basic Research Laboratory, under the direction of Dr. Hiroshi Matsuo, focuses on research to determine structures of protein-protein and protein-DNA or RNA complexes by using nuclear magnetic spectroscopy (NMR) and X-ray crystallography.  The section also develops new techniques in order to overcome current limitations in studying large and complicated macromolecular complexes.

JOB DESCRIPTION
The Post Doctoral Fellow will 1) perform laboratory research on human APOBEC3 proteins and HIV-1 Vif E3 ligase complex, 2) perform hands-on bench work with the expectation of producing first author papers, 3) performance of a full range of experiments from molecular biology to structural biology, 4) perform work that will involve several projects aimed at obtaining atomic-level understanding of the APOBEC3-VIf interaction, 5) perform NMR spectroscopy, data analysis and structure determination of the APOBEC3G-VIf E3 ligase complex, and 6) develop new methods to study structure and function of large multi-protein complexes using NMR.

Requirements

BASIC QUALIFICATIONS
Possession of a Doctoral degree from an accredited college or university according to the Council for Higher Education Accreditation (CHEA) appropriate to biomedical research
Foreign degrees must be evaluated for U.S. equivalency
Demonstrated experience in:  Three dimensional triple resonance NMR spectroscopy, expression and purification of stable isotope labeled protein, and protein structure determination using NMR data
Record of first-author publications
Scientific writing and presentation skills
PREFERRED QUALIFICATIONS
Reading and writing of NMR pulse sequences (Bruker or Varian)
Knowledge of virology of retroviluses such as HIV and biology of ubiquitine mediated protein degradation