Structure of linker molecules employed for biotin attachment to the stem–loop structures

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Immobilized stem–loop structured probes as conformational switches for enzymatic detection of microbial 16S rRNA"</p><p>Nucleic Acids Research 2005;33(11):e101-e101.</p><p>Published online 24 Jun 2005</p><p>PMCID:PMC1159122.</p><p>© The Author 2005. Published by Oxford University Press. All rights reserved</p> ARP-biotin [-(aminooxyacetyl)--(-biotinoyl)hydrazine] is attached via Schiff base chemistry to an aldehyde group generated by oxidative cleavage of the terminal ribose moiety of cytidin (rC). C3-Biotin contains a C3-ether-glycerol linker attached to the biotin residue via an amide bond. In TEG-biotin, the C3-ether-glycerol linker is extended by a triethyleneglycol (TEG) moiety

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