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

NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.

The Journal of biological chemistry - 13 Aug 2004

Santiveri Clara M, Pérez-Cañadillas José Manuel, Vadivelu Murali K, Allen Mark D, Rutherford Trevor J, Watkins Nicholas A, Bycroft Mark

Abstract excerpt

The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy. The protein native state shows conformational heterogeneity attributable to the isomerization of the peptide bond preceding a conserved proline residue. The two equally populated cis and trans forms both adopt an elongated antiparallel three alpha-helix bundle...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Blood Proteins

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

Share to Dimerization

Share to Gene Library

Share to Magnetic Resonance Spectroscopy

Share to Molecular Chaperones

Share to Proline

Share to Tyrosine

Source

Identifiers

PMID: 15178680
DOI: 10.1074/jbc.M405016200

Genes

AHSP

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

NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.PMID 15178680Read ↗

A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin.Semantic proximity Read ↗

Role of alpha-hemoglobin-stabilizing protein in normal erythropoiesis and beta-thalassemia.Semantic proximity Read ↗

Kinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate.Semantic proximity Read ↗

Dynamic Aha1 Co-Chaperone Binding to Human Hsp90Semantic proximity Read ↗

Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation.Semantic proximity Read ↗

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium.Semantic proximity Read ↗

NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms.Semantic proximity Read ↗

Analysis of human alpha globin gene mutations that impair binding to the alpha hemoglobin stabilizing protein.Semantic proximity Read ↗

Insights into hemoglobin assembly through in vivo mutagenesis of α-hemoglobin stabilizing protein.Semantic proximity Read ↗

Functional and NMR studies of Hb Sassari (Asp-126 alpha----His); role of the inter-subunit contacts in the affinity control of human hemoglobin.Semantic proximity Read ↗

The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface.Semantic proximity Read ↗

Local and global effects of a cavity filling mutation in a metastable serpin.Semantic proximity Read ↗

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