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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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Detalles Bibliográficos
Publicado en:Proc Natl Acad Sci U S A
Autores principales: Brünger, A T, Clore, G M, Gronenborn, A M, Karplus, M
Formato: Artigo
Lenguaje:Inglês
Publicado: National Academy of Sciences 1986
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Acceso en línea: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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