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

Domain behavior during the folding of a thermostable phosphoglycerate kinase.

Biochemistry - 10 Dec 1996

Parker M J, Spencer J, Jackson G S, Burston S G, Hosszu L L, Craven C J, Waltho J P, Clarke A R

Abstract excerpt

Bacillus stearothermophilus phosphoglycerate kinase (bsPGK) is a monomeric enzyme of 394 residues comprising two globular domains (N and C), covalently linked by an interdomain alpha-helix (residues 170-185). The molecule folds to the native state in three stages. In the first, each domain rapidl...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Stability
Share to Kinetics
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Polymerase Chain Reaction

Share to Protein Folding

Share to Recombinant Proteins

Share to Thermodynamics

Source

Identifiers

PMID: 8961937
DOI: 10.1021/bi961330s

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-8961937-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Domain behavior during the folding of a thermostable phosphoglycerate kinase.PMID 8961937Read ↗

The denatured state of N-PGK is compact and predominantly disordered.Semantic proximity Read ↗

Origin of conformational dynamics in a globular protein.Semantic proximity Read ↗

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

Folding kinetics of the cooperatively folded subdomain of the IκBα ankyrin repeat domain.Semantic proximity Read ↗

A thiol labelling competition experiment as a probe for sidechain packing in the kinetic folding intermediate of N-PGK.Semantic proximity Read ↗

Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein.Semantic proximity Read ↗

Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry.Semantic proximity Read ↗

Characterization of an intermediate in the folding pathway of phosphoglycerate kinase: chemical reactivity of genetically introduced cysteinyl residues during the folding process.Semantic proximity Read ↗

Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Semantic proximity Read ↗

Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.Semantic proximity Read ↗

Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.Semantic proximity Read ↗

Non-Native α-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the β-Barrel in β-Lactoglobulin.Semantic proximity Read ↗

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