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

The folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutant.

Biophysical journal - 5 May 2015

Ramírez-Sarmiento César A, Baez Mauricio, Zamora Ricardo A, Balasubramaniam Deepa, Babul Jorge, Komives Elizabeth A, Guixé Victoria

Abstract excerpt

Escherichia coli phosphofructokinase-2 (Pfk-2) is an obligate homodimer that follows a highly cooperative three-state folding mechanism N2 ↔ 2I ↔ 2U. The strong coupling between dissociation and unfolding is a consequence of the structural features of its interface: a bimolecular domain formed by intertwining of the small domain of each subunit into a flattened β-barrel. Although isolated monomers of E. coli...

Topics

Amino Acid Sequence
Escherichia coli
Escherichia coli Proteins
Molecular Sequence Data
Mutation
Phosphofructokinase-2
Protein Folding
Protein Multimerization
Protein Structure, Tertiary
Protein Subunits

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 25954892
DOI: 10.1016/j.bpj.2015.04.001
PMCID: PMC4423062

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutant.PMID 25954892Read ↗

Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency.Semantic proximity Read ↗

Dual allosteric activation mechanisms in monomeric human glucokinase.Semantic proximity Read ↗

NEXT-FRET: A solution-based smFRET platform to resolve folding intermediates under native conditionsSemantic proximity Read ↗

Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations.Semantic proximity Read ↗

Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder.Semantic proximity Read ↗

Association and activation of fructose 1,6-bisphosphase during unfolding and refolding: spectroscopic and enzymatic studies.Semantic proximity Read ↗

Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution.Semantic proximity Read ↗

Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.Semantic proximity Read ↗

Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2,6-bisphosphate allosteric site of mammalian phosphofructokinase.Semantic proximity Read ↗

A single point mutation leads to an instability of the hetero-octameric structure of yeast phosphofructokinase.Semantic proximity Read ↗

Protein GB1 folding and assembly from structural elements.Semantic proximity Read ↗

Mutations in the tetramer interface of human glucose-6-phosphate dehydrogenase reveals kinetic differences between oligomeric states.Semantic proximity Read ↗

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