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

Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America - 19 Jun 2007

Chen Huimin, Rhoades Elizabeth, Butler James S, Loh Stewart N, Webb Watt W

Abstract excerpt

The spectra of equilibrium chain conformation fluctuations of apomyoglobin (apoMb) as a function of folding, from the acid-denatured state at pH 2.6 through the stable molten globule state pH approximately 4.1 to the folded state at pH 6.3, are reported, as measured by fluorescence correlation spectroscopy. The conformational fluctuations, which are detected by quenching of an N-terminal fluorescent label by...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Diffusion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Myoglobin

Share to Protein Denaturation

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 17556539
DOI: 10.1073/pnas.0704073104
PMCID: PMC1965535

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

Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy.PMID 17556539Read ↗

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

Sequence determinants of a protein folding pathway.Semantic proximity Read ↗

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

Misfolding and amyloid aggregation of apomyoglobin.Semantic proximity Read ↗

Sampling unfolding intermediates in calmodulin by single-molecule spectroscopy.Semantic proximity Read ↗

Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.Semantic proximity Read ↗

Snapshots of a protein folding intermediate.Semantic proximity Read ↗

Similarity of force-induced unfolding of apomyoglobin to its chemical-induced unfolding: an atomistic molecular dynamics simulation approach.Semantic proximity Read ↗

Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutants.Semantic proximity Read ↗

Molecular mechanism underlying the thermal stability and pH-induced unfolding of CHABII.Semantic proximity Read ↗

The role of Trp-82 in the folding of intestinal fatty acid binding protein.Semantic proximity Read ↗

[Kinetics of interaction between apomyoglobin and phospholipid membrane].Semantic proximity Read ↗

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