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Aptamers are nucleic acid molecules that bind to a target molecule with high affinity and specificity, which are generated by a process known as systematic evolution of ligands by exponential enrichment (SELEX). Because of their high affinity and specificity, aptamers were developed as therapeutic agents. Although aptamers are investigated as promising therapeutic agents, the mechanism of their high affinity and specificity is not clear. Therefore, structural and biophysical studies are important to know that. To date, ITC is increasingly being used to study the thermodynamic basis of aptamer-target protein interactions. Understanding the mechanism of aptamer binding would contribute to their development for therapeutic applications. In this chapter, we describe the protocol to study the thermodynamics of aptamer-protein interactions.
This article was published in the following journal.
Name: Methods in molecular biology (Clifton, N.J.)
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Nucleotide sequences, generated by iterative rounds of SELEX APTAMER TECHNIQUE, that bind to a target molecule specifically and with high affinity.
Peptide sequences, generated by iterative rounds of SELEX APTAMER TECHNIQUE, that bind to a target molecule specifically and with high affinity.
A family of endogenous regulatory proteins that associate with RETINOBLASTOMA PROTEIN via a specific high-affinity binding domain. Members of this family of proteins are often found associated with histone-modifying enzymes and protein complexes that regulate gene expression.
A family of RNA-BINDING PROTEINS that contain an RNA RECOGNITION MOTIF and two ribonucleoprotein (RNP) domains which bind RNA, in addition to other domains that allow for high affinity binding, sequence specificity, and protein interactions. Examples of RNA recognition motif proteins include HETEROGENEOUS NUCLEAR RIBONUCLEARPROTEINS (hnRNP) and EMBRYONIC LETHAL ABNORMAL-VISION (ELAV) proteins.
A heterodimeric protein complex of RNA cap-binding proteins, which binds with high affinity to the 5' MRNA CAP STRUCTURE in the CELL NUCLEUS. The complex contains two subunits, one of 80-kDa molecular weight and another of 20-kDa molecular weight.
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