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

Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor.

Biophysical chemistry - 1 Jan 2003

Anderson Thomas A, Sauer Robert T

Abstract excerpt

The Arc repressor of bacteriophage P22 is a member of the ribbon-helix-helix family of transcription factors. Ser32 is a solvent-exposed position that serves a structural role as the N(cap) residue of alpha-helix B of Arc, but also serves a functional role because its side chain is packed close to the sugar-phosphate DNA backbone in the repressor-operator complex. The tolerance of this N(cap) position to...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophage P22
Share to Chemical Phenomena
Share to Chemistry, Physical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoretic Mobility Shift Assay

Share to Hot Temperature

Share to Operator Regions, Genetic

Share to Solvents

Share to Viral Regulatory and Accessory Proteins

Source

Identifiers

PMID: 12646376
DOI: 10.1016/s0301-4622(02)00291-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor.PMID 12646376Read ↗

Sequence determinants of a conformational switch in a protein structure.Semantic proximity Read ↗

A polymetamorphic protein.Semantic proximity Read ↗

Dual regulation of open-complex formation and promoter clearance by Arc explains a novel repressor to activator switch.Semantic proximity Read ↗

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

The ArcB leucine zipper domain is required for proper ArcB signaling.Semantic proximity Read ↗

Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence.Semantic proximity Read ↗

P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences.Semantic proximity Read ↗

Protein linear indices of the 'macromolecular pseudograph alpha-carbon atom adjacency matrix' in bioinformatics. Part 1: prediction of protein stability effects of a complete set of alanine substitutions in Arc repressor.Semantic proximity Read ↗

The energetic contribution of backbone--backbone hydrogen bonds to the thermodynamic stability of a hyperstable P22 Arc repressor mutant.Semantic proximity Read ↗

A single P115Q mutation modulates specificity in the Corynebacterium pseudotuberculosis arginine repressor.Semantic proximity Read ↗

Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex.Semantic proximity Read ↗

Investigation of arc repressor DNA-binding specificity by comparative molecular dynamics simulations.Semantic proximity Read ↗

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