Abstract
Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.
| Original language | English |
|---|---|
| Pages (from-to) | 635-642 |
| Number of pages | 8 |
| Journal | Current Opinion in Structural Biology |
| Volume | 9 |
| Issue number | 5 |
| DOIs | |
| State | Published - Oct 1 1999 |
Bibliographical note
Funding Information:We thank Roberto Tejero and Yuanpeng Huang for useful discussions and Rebecca Watson for her expert assistance in scientific editing. The authors’ work on automated analysis is supported by grants from the National Institutes of Health (GM-47014), the National Science Foundation (MCB-9407569 and MCB-9357526) and by a New Jersey Commission on Science and Technology Research Excellence Award.
Funding
We thank Roberto Tejero and Yuanpeng Huang for useful discussions and Rebecca Watson for her expert assistance in scientific editing. The authors’ work on automated analysis is supported by grants from the National Institutes of Health (GM-47014), the National Science Foundation (MCB-9407569 and MCB-9357526) and by a New Jersey Commission on Science and Technology Research Excellence Award.
| Funders | Funder number |
|---|---|
| National Science Foundation (NSF) | MCB-9357526, MCB-9407569 |
| National Institutes of Health (NIH) | GM-47014 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
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