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The exocyclic amine at the RNase P cleavage site contributes to substrate binding and catalysis.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
2006 (English)In: J Mol Biol, ISSN 0022-2836, Vol. 359, no 3, 572-84 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2006. Vol. 359, no 3, 572-84 p.
Keyword [en]
Amines/*chemistry, Base Pairing, Base Sequence, Binding Sites, Catalysis, Guanosine/*chemistry, Hydroxides/chemistry, Magnesium/chemistry, Molecular Sequence Data, Mutation, Nitrogen/chemistry, Nucleic Acid Conformation, Oxygen/chemistry, Protein Binding, RNA; Transfer/chemistry/genetics, Ribonuclease P/*chemistry, Substrate Specificity
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URN: urn:nbn:se:uu:diva-23267PubMedID: 16638615OAI: oai:DiVA.org:uu-23267DiVA: diva2:51041
Available from: 2007-01-26 Created: 2007-01-26 Last updated: 2011-01-11

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