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The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.

The polypeptide fold of the 79-residue globular domain of chicken histone H5 (GH5) in solution has been determined by the combined use of distance geometry and restrained molecular dynamics calculations. The structure determination is based on 307 approximate interproton distance restraints derived...

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Dades bibliogràfiques
Publicat a:EMBO J
Autors principals: Clore, G M, Gronenborn, A M, Nilges, M, Sukumaran, D K, Zarbock, J
Format: Artigo
Idioma:Inglês
Publicat: Nature Publishing Group 1987
Matèries:
Accés en línia:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC553562/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3608994/
https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1987.tb02438.x
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