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

Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.

The journal of physical chemistry. B - 13 Dec 2018

Mizukami Takuya, Xu Ming, Fazlieva Ruzaliya, Bychkova Valentina E, Roder Heinrich

Abstract excerpt

Under mildly acidic conditions (pH 4-4.5) apomyoglobin (apoMb) adopts a partially structured equilibrium state ( M-state) that structurally resembles a kinetic intermediate encountered at a late stage of folding to the native structure at neutral pH. We have previously reported that the M-state is formed rapidly (<1 ms) via a multistate process and thus offers a unique opportunity for exploring early stages of...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Hydrogen-Ion Concentration

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

Share to Hydrophobic and Hydrophilic Interactions

Share to Mutagenesis, Site-Directed

Share to Myoglobin

Share to Protein Conformation, alpha-Helical

Share to Protein Unfolding

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 30133301
DOI: 10.1021/acs.jpcb.8b06895
PMCID: PMC6395567

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

Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.PMID 30133301Read ↗

Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy.Semantic proximity Read ↗

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

Insights into protein folding mechanisms from large scale analysis of mutational effects.Semantic proximity Read ↗

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

Mutational Analysis of Protein Folding Transition States: Phi Values.Semantic proximity Read ↗

Microsecond protein folding through a compact transition state.Semantic proximity Read ↗

Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.Semantic proximity Read ↗

Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain.Semantic proximity Read ↗

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

Transient folding intermediates characterized by protein engineering.Semantic proximity Read ↗

Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations.Semantic proximity Read ↗

Atomistic folding simulations of the five-helix bundle protein λ(6−85).Semantic proximity Read ↗

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