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

Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange.

Journal of molecular biology - 18 Dec 1998

Englander J J, Louie G, McKinnie R E, Englander S W

Abstract excerpt

A hydrogen exchange (HX) functional labeling method was used to study allosterically active segments in human hemoglobin (Hb) at the alpha-chain N terminus and the beta-chain C terminus. Allosterically important interactions that contact these segments were removed one or more at a time by mutation (Hbs Cowtown, Bunbury, Barcelona, Kariya), proteolysis (desArg141alpha, desHis146beta), chemical modification...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Chlorides
Share to Cross-Linking Reagents

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

Share to Hemoglobins

Share to Histidine

Share to Mutation

Share to Phosphates

Share to Protein Conformation

Source

Identifiers

PMID: 9878380
DOI: 10.1006/jmbi.1998.2278

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

Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange.PMID 9878380Read ↗

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 ↗

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.Semantic proximity Read ↗

Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamics.Semantic proximity Read ↗

Site-directed mutations of human hemoglobin at residue 35beta: a residue at the intersection of the alpha1beta1, alpha1beta2, and alpha1alpha2 interfaces.Semantic proximity Read ↗

On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin.Semantic proximity Read ↗

Molecular code for cooperativity in hemoglobin.Semantic proximity Read ↗

50 years of allosteric interactions: the twists and turns of the models.Semantic proximity Read ↗

Recombinant hemoglobins with low oxygen affinity and high cooperativity.Semantic proximity Read ↗

Functional properties of human hemoglobins synthesized from recombinant mutant beta-globins.Semantic proximity Read ↗

Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling.Semantic proximity Read ↗

Is cooperative oxygen binding by hemoglobin really understood?Semantic proximity Read ↗

Site-specific hydrogen exchange of proteins: insights into the structures of amyloidogenic intermediates.Semantic proximity Read ↗

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