Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

RNA affinity for molecular L-histidine; genetic code origins.

Journal of molecular evolution - 1 Aug 2005

Majerfeld Irene, Puthenvedu Deepa, Yarus Michael

Abstract excerpt

Selection for affinity for free histidine yields a single RNA aptamer, which was isolated 54 times independently. This RNA is highly specific for the side chain and binds protonated L-histidine with 10(2)-10(3)-fold stereoselectivity and a dissociation constant (K(D)) of 8-54 microM in different isolates. These histidine-binding RNAs have a common internal loop-hairpin loop structure, based on a conserved...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Aptamers, Nucleotide
Share to Chromatography, Affinity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Code

Share to Histidine

Share to Hydrogen-Ion Concentration

Share to Nucleic Acid Conformation

Source

Identifiers

PMID: 15999244
DOI: 10.1007/s00239-004-0360-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

RNA affinity for molecular L-histidine; genetic code origins.PMID 15999244Read ↗

A Highly Specific DNA Aptamer for RNase H2 from Clostridium difficileSemantic proximity Read ↗

A target-unrelated peptide in an M13 phage display library traced to an advantageous mutation in the gene II ribosome-binding site.Semantic proximity Read ↗

Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding.Semantic proximity Read ↗

An uncommon [K+(Mg2+)2] metal ion triad imparts stability and selectivity to the Guanidine-I riboswitch.Semantic proximity Read ↗

Guanine riboswitch variants from Mesoplasma florum selectively recognize 2'-deoxyguanosine.Semantic proximity Read ↗

Nucleotide sequence of the Escherichia coli K12 histidine operon revisited.Semantic proximity Read ↗

Bacterial aptamers that selectively bind glutamine.Semantic proximity Read ↗

In vitro selection for altered divalent metal specificity in the RNase P RNA.Semantic proximity Read ↗

Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch.Semantic proximity Read ↗

Retention of function in the DNA homolog of the RNA dopamine aptamer.Semantic proximity Read ↗

Synthesis of a novel histidine analogue and its efficient incorporation into a protein in vivo.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.