reference/15825886

http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15825886

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endingPage	2842
issn	0006-2960 1520-4995
issueIdentifier	10
pageRange	2838-2842
publicationName	Biochemistry
startingPage	2838
bibliographicCitation	Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L. 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1. Biochemistry. 1994 Mar 15;33(10):2838–42. doi: 10.1021/bi00176a013. PMID: 8130196.
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date	1994-03-15-04:00^^<http://www.w3.org/2001/XMLSchema#date>
identifier	https://pubmed.ncbi.nlm.nih.gov/8130196 https://doi.org/10.1021/bi00176a013
isPartOf	http://rdf.ncbi.nlm.nih.gov/pubchem/journal/1028 https://portal.issn.org/resource/ISSN/0006-2960 https://portal.issn.org/resource/ISSN/1520-4995
language	English
source	https://pubmed.ncbi.nlm.nih.gov/ https://www.crossref.org/
title	1H NMR Studies of Mouse Ribonucleotide Reductase: The R2 Protein Carboxyl-Terminal Tail, Essential for Subunit Interaction, Is Highly Flexible but becomes Rigid in the Presence of Protein R1
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Total number of triples: 50.