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

Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation.

Journal of molecular biology - 8 Apr 2005

Ferguson Neil, Day Ryan, Johnson Christopher M, Allen Mark D, Daggett Valerie, Fersht Alan R

Abstract excerpt

We used Phi-value analysis to characterise the transition state for folding of a thermophilic protein at the relatively high temperature of 325 K. PhiF values for the folding of the three-helix bundle, peripheral subunit binding domain from Bacillus stearothermophilus (E3BD) were determined by temperature-jump experiments in the absence of chemical denaturants. E3BD folded in microseconds through a highly diffuse...

Read the complete abstract on PubMed

Topics

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

Share to Calorimetry, Differential Scanning
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Geobacillus stearothermophilus

Share to Hot Temperature

Share to Hydrogen Bonding

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Denaturation

Share to Thermodynamics

Source

Identifiers

PMID: 15769475
DOI: 10.1016/j.jmb.2004.12.061

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

Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation.PMID 15769475Read ↗

Phi-value analysis and the nature of protein-folding transition states.Semantic proximity Read ↗

Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Semantic proximity Read ↗

How general is the nucleation-condensation mechanism?Semantic proximity Read ↗

The structure of the major transition state for folding of an FF domain from experiment and simulation.Semantic proximity Read ↗

Time-resolved backbone desolvation and mutational hot spots in folding proteins.Semantic proximity Read ↗

Phi-analysis of the folding of the B domain of protein A using multiple optical probes.Semantic proximity Read ↗

Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding.Semantic proximity Read ↗

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Unspecific hydrophobic stabilization of folding transition states.Semantic proximity Read ↗

Phi-analysis at the experimental limits: mechanism of beta-hairpin formation.Semantic proximity Read ↗

Unfolding of the cold shock protein studied with biased molecular dynamics.Semantic proximity Read ↗

The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy.Semantic proximity Read ↗

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