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

Lac repressor hinge flexibility and DNA looping: single molecule kinetics by tethered particle motion.

Nucleic acids research - 1 Jan 2006

Vanzi Francesco, Broggio Chiara, Sacconi Leonardo, Pavone Francesco Saverio

Abstract excerpt

The tethered particle motion (TPM) allows the direct detection of activity of a variety of biomolecules at the single molecule level. First pioneered for RNA polymerase, it has recently been applied also to other enzymes. In this work we employ TPM for a systematic investigation of the kinetics of DNA looping by wild-type Lac repressor (wt-LacI) and by hinge mutants Q60G and Q60 + 1. We implement a novel method...

Read the complete abstract on PubMed

Topics

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

Share to Kinetics
Share to Lac Operon
Share to Lac Repressors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microspheres

Share to Motion

Share to Nucleic Acid Conformation

Share to Operator Regions, Genetic

Share to Repressor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16835309
DOI: 10.1093/nar/gkl393
PMCID: PMC1524907

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 · 12 closest

Lac repressor hinge flexibility and DNA looping: single molecule kinetics by tethered particle motion.PMID 16835309Read ↗

Escherichia coli processivity clamp β from DNA polymerase III is dynamic in solution.Semantic proximity Read ↗

ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.Semantic proximity Read ↗

The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes related to DNA binding.Semantic proximity Read ↗

Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex.Semantic proximity Read ↗

The time scale of the catalytic loop motion in triosephosphate isomerase.Semantic proximity Read ↗

Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Semantic proximity Read ↗

Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity.Semantic proximity Read ↗

A ratchet mechanism of transcription elongation and its control.Semantic proximity Read ↗

ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuationsSemantic proximity Read ↗

LacI strikes a balance between stability and inducibility.Semantic proximity Read ↗

Scaling the Dynamics of Coiled CoilsSemantic proximity Read ↗

Tuned SMC Arms Drive Chromosomal Loading of Prokaryotic Condensin.Semantic proximity Read ↗

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