Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 19, Issue 2, Pages 145-155Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2009.02.005
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Funding
- Alfred P Sloan Foundation
- NSF [DBI 0746198]
- National Institute of General Medical Sciences [R01GM083107]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM083107] Funding Source: NIH RePORTER
- Div Of Biological Infrastructure [1027394, 0746198] Funding Source: National Science Foundation
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Computationally predicted three-dimensional structure of protein molecules has demonstrated the usefulness in many areas of biomedicine, ranging from approximate family assignments to precise drug screening. For nearly 40 years, however, the accuracy of the predicted models has been dictated by the availability of close structural templates. Progress has recently been achieved in refining low-resolution models closer to the native ones; this has been made possible by combining knowledge-based information from multiple sources of structural templates as well as by improving the energy funnel of physics-based force fields. Unfortunately, there has been no essential progress in the development of techniques for detecting remotely homologous templates and for predicting novel protein structures.
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