Functional dynamics in the active site of the ribonuclease binase

Binase, a member of a family of microbial guanyl-specific ribonucleases, catalyzes the endonucleotic cleavage of single-stranded RNA. It shares 82% amino acid identity with the well-studied protein barnase. We used NMR spectroscopy to study the millisecond dynamics of this small enzyme, using severa...

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Veröffentlicht in:	Proc Natl Acad Sci U S A
Hauptverfasser:	Wang, Lincong, Pang, Yuxi, Holder, Tina, Brender, Jeffrey R., Kurochkin, Alexander V., Zuiderweg, Erik R. P.
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	National Academy of Sciences 2001
Schlagworte:	Biological Sciences
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC35402/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11438724/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.121069998
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Functional dynamics in the active site of the ribonuclease binase

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