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

Force field dependence of riboswitch dynamics.

Methods in enzymology - 1 Jan 2015

Hanke Christian A, Gohlke Holger

Abstract excerpt

Riboswitches are noncoding regulatory elements that control gene expression in response to the presence of metabolites, which bind to the aptamer domain. Metabolite binding appears to occur through a combination of conformational selection and induced fit mechanism. This demands to characterize t...

Read the complete abstract on PubMed

Topics

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

Share to Magnesium
Share to Aptamers, Nucleotide
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Nucleic Acid Conformation

Share to Riboswitch

Source

Identifiers

PMID: 25726465
DOI: 10.1016/bs.mie.2014.10.056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25726465-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Force field dependence of riboswitch dynamics.PMID 25726465Read ↗

Ligand Selectivity Mechanism and Conformational Changes in Guanine Riboswitch by Molecular Dynamics Simulations and Free Energy Calculations.Semantic proximity Read ↗

Ligand Binding Mechanism and Its Relationship with Conformational Changes in Adenine Riboswitch.Semantic proximity Read ↗

Ligand-mediated and tertiary interactions cooperatively stabilize the P1 region in the guanine-sensing riboswitch.Semantic proximity Read ↗

Interplay of 'induced fit' and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch.Semantic proximity Read ↗

A cooperative effect of ligands, Mg2+ ions, and the U6C mutation on the structural dynamics of the SAM-Ⅵ Riboswitch.Semantic proximity Read ↗

In-silico studies on thermodynamics of ligand binding to Fluoride riboswitch aptamerSemantic proximity Read ↗

Dissecting the influence of Mg2+ on 3D architecture and ligand-binding of the guanine-sensing riboswitch aptamer domain.Semantic proximity Read ↗

Thermodynamic and kinetic characterization of ligand binding to the purine riboswitch aptamer domain.Semantic proximity Read ↗

Influence of ground-state structure and Mg2+ binding on folding kinetics of the guanine-sensing riboswitch aptamer domain.Semantic proximity Read ↗

Molecular dynamics study of the recognition of ATP by nucleic acid aptamers.Semantic proximity Read ↗

Tuning strand displacement kinetics enables programmable ZTP riboswitch dynamic range in vivo.Semantic proximity Read ↗

Insights into the ligand-free structure of cyclic diguanosine monophosphate I riboswitch of <i>Vibrio cholerae</i> using molecular dynamics simulationSemantic proximity Read ↗

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