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

P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate.

Biochemistry - 15 Nov 2005

Meinhold Derrick, Boswell Sarah, Colón Wilfredo

Abstract excerpt

The factor for inversion stimulation (FIS) is a homodimeric DNA-binding protein found in enteric bacteria. FIS consists of 98 residues and self-assembles into an entwined dimer containing a flexible and mostly disordered N-terminus followed by four alpha-helices. Proline 61, which is 100% conserved in FIS homologues, is located at the center of helix B, and its substitution for alanine (P61A) was previously shown...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Cross-Linking Reagents
Share to Dimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Proline

Share to Protein Denaturation

Share to Temperature

Source

Identifiers

PMID: 16274219
DOI: 10.1021/bi050640k

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate.PMID 16274219Read ↗

The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity.Semantic proximity Read ↗

The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue.Semantic proximity Read ↗

Structural analysis of the transcriptional activation region on Fis: crystal structures of six Fis mutants with different activation properties.Semantic proximity Read ↗

Conformational stability of the bacterial adhesin, FimH, with an inactivating mutation.Semantic proximity Read ↗

A Mutation Directs the Structural Switch of DNA Binding Proteins under Starvation to a Ferritin-like Protein Cage.Semantic proximity Read ↗

Stable folding core in the folding transition state of an alpha-helical integral membrane protein.Semantic proximity Read ↗

Engineering a compact non-native state of intestinal fatty acid-binding protein.Semantic proximity Read ↗

An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.Semantic proximity Read ↗

Conversion of a beta-strand to an alpha-helix induced by a single-site mutation observed in the crystal structure of Fis mutant Pro26Ala.Semantic proximity Read ↗

Intermolecular interactions between cysteine and aromatic amino acids with phenyl moiety in the DNA-binding domain of heat shock factor 1 regulate thermal stress-induced trimerizationSemantic proximity Read ↗

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

Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.Semantic proximity Read ↗

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