Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin.
Model calculations are performed to evaluate the utility of molecular dynamics with NMR interproton distance restraints for determining the three-dimensional structure of proteins. The system used for testing the method is the 1.5-A resolution crystal structure of crambin (a protein of 46 residues)...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1986
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC323611/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3459158/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.83.11.3801 |
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