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

Helix mutations stabilize a late productive intermediate on the folding pathway of ubiquitin.

Biochemistry - 5 Aug 2008

Rea Anita M, Simpson Emma R, Crespo Maria D, Searle Mark S

Abstract excerpt

We have investigated the relative placement of rate-limiting energy barriers and the role of productive or obstructive intermediates on the folding pathway of yeast wild-type ubiquitin ( wt-Ub) containing the F45W mutation. To manipulate the folding barriers, we have designed a family of mutants in which stabilizing substitutions have been introduced incrementally on the solvent-exposed surface of the main...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Magnetic Resonance Spectroscopy
Share to Protein Denaturation

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

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Temperature

Share to Thermodynamics

Share to Ubiquitin

Source

Identifiers

PMID: 18616284
DOI: 10.1021/bi800722d

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Helix mutations stabilize a late productive intermediate on the folding pathway of ubiquitin.PMID 18616284Read ↗

Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues.Semantic proximity Read ↗

Population of on-pathway intermediates in the folding of ubiquitin.Semantic proximity Read ↗

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

The Trajectory Taken by Dimeric Cu/Zn Superoxide Dismutase Through the Protein Unfolding and Dissociation Landscape Is Modulated by Salt-Bridge FormationSemantic proximity Read ↗

High-Resolution Mapping of the Folding Transition State of a WW Domain.Semantic proximity Read ↗

Identification of a key structural element for protein folding within beta-hairpin turns.Semantic proximity Read ↗

Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer.Semantic proximity Read ↗

Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism.Semantic proximity Read ↗

A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble.Semantic proximity Read ↗

Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates.Semantic proximity Read ↗

GROEL/ES Buffers Entropic Traps in Folding Pathway during Evolution of a Model Substrate.Semantic proximity Read ↗

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