Freedom of Information Act Office
IC Directors' Meeting Highlights
April 24, 2006
|From:||Director, Executive Secretariat|
|Subject:||IC Directors Meeting Highlights—December 22, 2005|
I. Workforce Planning
Ms. Barros began by providing background on the broad NIH strategic workforce planning effort that includes factors influencing workforce planning and future workforce needs to fulfill the NIH mission in advancing medical research. Ms. Barros provided information on the environmental challenges and the drivers, both internal and external, that are impacting NIH's workforce needs, ranging from various Acts of Congressional Legislation to ambitious Government-wide programs such as the President's Management Agenda established by the current administration. These include: bio-terrorism, pandemic flu, unanticipated health crises, NIH Roadmap, Neuroscience Blue-print, OPASI, GPRA, HHS Top 20 Management Objectives, and emergency response requirements.
Ms. Barros presented an assessment of the current NIH workforce derived from existing data to begin identifying potential areas of other significant challenges highlighted by factors like age distribution, turnover statistics, retirement eligibility, overall NIH population, and demographic trends. To assist in developing a future-oriented plan, NIH has selected Tunnell Consulting whose collaborative approach, experience in this area, and staff, which blends science, business, and academic expertise, all render it well suited to guiding NIH through the process. Tunnell staff has identified best practices institutions that have successfully addressed similar challenges to the NIH in management of their human capital. Staff will follow up with interviews and workshops with each IC to find similar patterns and to collect specific data. While the current effort focused on Phase I and the FY 2006 staffing goals, phases II and II will expand upon the information to include analysis of trends over the past five years and an assessment of additional aspects of the workforce.
II. New Investigators Ad Hoc Committee on a Proposed Career Transition Awards Program
Drs. Landis and Ruiz-Bravo reported on the work of the ad hoc subcommittee of the NIH Steering Committee charged with looking at a proposed career transition award program for new investigators that will help increase and maintain a healthy cohort of new and talented, NIH-supported, independent investigators and facilitate an investigator’s ability get her first RO1 award earlier in her career.
NIH will issue between 150 and 200 awards for this program in its initial year, beginning in fall 2006. It expects to issue the same number of awards each of the following five years. During this time, the NIH will provide almost $400 million in support of the program. This award is a major piece of a larger, ongoing NIH effort to support new scientists as they transition to research independence. All NIH Institutes and Centers are participating in this award program.
The award will work as follows: The initial 1-2 year mentored phase will allow investigators to complete their supervised research work, publish results, and search for an independent research position. The second, independent phase, years 3-5, will allow awardees who secure an assistant professorship, or equivalent position, to establish their own research program and successfully apply for an NIH Investigator-Initiated (R01) grant. The R01 is the major means by which NIH supports individual scientists in the field.
The group discussed various issues including how to best ensure that all applications are reviewed fairly and effectively.
Dr. Zerhouni requested that ICs follow-up with Drs. Landis and Ruiz-Bravo and that the Committee then move forward promptly.
Note: The Pathways to Independence Program was announced on January 27, 2005. See http://grants2.nih.gov/grants/new_investigators/index.htm
III. Protein Structure Determination: From Myoglobin to Modeling the Human Proteome
Dr. Berg traced the history of protein structure determination by X-ray diffraction methods from the 1895 discovery of X-ray technology through 1957 when Nobel laureate John Kendruw solved the structure of myoglobin and 1960 when Nobel laureate Max Prutz solved the structure of hemoglobin. He then discussed the subsequent advances noting that high resolution three-dimensional X-ray analysis and new technology led to physical models showing that myoglobin and hemoglobin chains have similar structures and that increasingly sophisticated three-dimensional structural analysis has revealed relationships undetectable by sequence comparison alone.
In 1971, the Brookhaven Laboratory founded the Protein Data Bank (PDB), which originally contained seven structures. In 1998, the Research Collaboratory for Structural Bioinformatics (RCSB) took over the management of the PDB. In addition to NSF and DOE, several ICs (NIGMS, NLM, NCI, NCRR, NIBIB, and NINDS) support this effort. The PDB is the single worldwide depository of information about the three-dimensional structures of large biological molecules, including proteins and nucleic acids and now contains upwards of 35,000 structures. Dr. Berg also mentioned additional research resources available to the research community online: the Pharmacogenetics Research Network (co-funded by NIGMS, NHLBI, NIDA, NCI, NIEHS, NIMH, NHGRI, NLM, and ORWH) and PharmGKB.
Dr. Berg explained the NIGMS’s Protein Structure Initiative and its proposed phase II. See http://www.nigms.nih.gov/Initiatives/PSI/. Since its inception, PSC Centers have determined 1303 structures. The PSI structures are available on the National Center for Biotechnology Web site: http://www.ncbi.nlm.nih.gov.
Concluding his presentation with exciting questions about the feasibility of modeling unknown protein structures, Dr. Berg discussed Nobel Laureate Christian Anfinsin’s research at NIH on the structure and composition of proteins and the Levinthal (Cyrus) Paradox: the observation that proteins fold into their specific three-dimensional conformations in a time span that is much shorter than would be possible if the molecule actually searched the entire conformation space for the lowest energy state. Citing two 2005 publications (J. Moult et al. in Proteins, Function, and Bioinformatics, and P. Bradley, K., Misura, and D. Baker in Science), Dr. Berg ended the discussion on the future of protein structural biology.
cc: OD Senior Staff