NIGMS Invites Biologists to Join High-Throughput Structure Initiative
Want to listen to this article for FREE?
Complete the form below to unlock access to ALL audio articles.
Read time: 1 minute
The National Institute of General Medical Sciences, part of the National Institutes of Health, has announced plans for a new direction of the Protein Structure Initiative, a structural genomics effort started in 2000.
As suggested by its new name, PSI:Biology, the program will support research partnerships between groups of biologists and high-throughput structure determination centers to solve problems of biomedical importance.
"This is a natural evolution for the PSI," said NIGMS Director Jeremy M. Berg, Ph.D. "The previous phases of the initiative developed a very efficient high-throughput structure determination pipeline along with other technologies to study the relationships between protein sequences and structures. Now, we want to foster the use of these technologies to explore a broad range of important biomedical research questions."
To this end, PSI:Biology will include eight components that will function in a highly interactive network.
Beginning in April 2009, NIGMS plans to release requests for applications for the following five components, which will be awarded beginning in July 2010 with an estimated fiscal year 2010 total budget of $37 million or more:
• High-throughput structure determination centers that will devote most of their efforts to solving community-nominated sets of protein structures, working with consortia of researchers outside of the centers and extending high-throughput technologies to increasingly complex structures;
• Consortia of scientists that will work with the structure determination centers to solve biological problems that require the solution of many protein structures, benefit from high-throughput technologies and drive additional technology development;
• Centers focused on determining membrane protein structures of great biological interest and on developing new methods to make these structures more amenable to high-throughput determination;
• The PSI-SG Knowledgebase, which will continue to play an integral role in information dissemination, the coordination of activities across the research network and the solicitation of community-nominated targets; and
• The PSI-SG Materials Repository, which will continue to serve the entire biomedical community by centralizing, maintaining, storing and distributing vectors and clones generated by PSI-supported researchers.
The PSI:Biology program was developed after extensive discussions with the research community about the future of the structural genomics field and how NIGMS can support its progress and after an assessment of the PSI. The plan was reviewed and approved by the National Advisory General Medical Sciences Council during its meeting on January 23, 2009.
At the meeting, council member Steven McKnight of the University of Texas Southwestern Medical Center at Dallas called PSI:Biology "a challenge to biologists to develop research programs that can take advantage of the fantastic resource for structure determination that NIGMS has put in place."
To date, PSI-supported researchers have generated more than 3,500 structures, many revealing novel patterns of folding. These findings as well as descriptions of new methods and technologies - some of which have been commercialized and are being used in labs around the world - have been reported in more than 1,200 research papers.
"We expect PSI:Biology to add to this rich history of protein structure determination by creating more opportunities for a broader range of scientists to collaborate and contribute new ideas," said Berg.
As suggested by its new name, PSI:Biology, the program will support research partnerships between groups of biologists and high-throughput structure determination centers to solve problems of biomedical importance.
"This is a natural evolution for the PSI," said NIGMS Director Jeremy M. Berg, Ph.D. "The previous phases of the initiative developed a very efficient high-throughput structure determination pipeline along with other technologies to study the relationships between protein sequences and structures. Now, we want to foster the use of these technologies to explore a broad range of important biomedical research questions."
To this end, PSI:Biology will include eight components that will function in a highly interactive network.
Beginning in April 2009, NIGMS plans to release requests for applications for the following five components, which will be awarded beginning in July 2010 with an estimated fiscal year 2010 total budget of $37 million or more:
• High-throughput structure determination centers that will devote most of their efforts to solving community-nominated sets of protein structures, working with consortia of researchers outside of the centers and extending high-throughput technologies to increasingly complex structures;
• Consortia of scientists that will work with the structure determination centers to solve biological problems that require the solution of many protein structures, benefit from high-throughput technologies and drive additional technology development;
• Centers focused on determining membrane protein structures of great biological interest and on developing new methods to make these structures more amenable to high-throughput determination;
• The PSI-SG Knowledgebase, which will continue to play an integral role in information dissemination, the coordination of activities across the research network and the solicitation of community-nominated targets; and
• The PSI-SG Materials Repository, which will continue to serve the entire biomedical community by centralizing, maintaining, storing and distributing vectors and clones generated by PSI-supported researchers.
The PSI:Biology program was developed after extensive discussions with the research community about the future of the structural genomics field and how NIGMS can support its progress and after an assessment of the PSI. The plan was reviewed and approved by the National Advisory General Medical Sciences Council during its meeting on January 23, 2009.
At the meeting, council member Steven McKnight of the University of Texas Southwestern Medical Center at Dallas called PSI:Biology "a challenge to biologists to develop research programs that can take advantage of the fantastic resource for structure determination that NIGMS has put in place."
To date, PSI-supported researchers have generated more than 3,500 structures, many revealing novel patterns of folding. These findings as well as descriptions of new methods and technologies - some of which have been commercialized and are being used in labs around the world - have been reported in more than 1,200 research papers.
"We expect PSI:Biology to add to this rich history of protein structure determination by creating more opportunities for a broader range of scientists to collaborate and contribute new ideas," said Berg.
