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

Structures of R- and T-state hemoglobin Bassett: elucidating the structural basis for the low oxygen affinity of a mutant hemoglobin.

Acta crystallographica. Section D, Biological crystallography - 1 Feb 2005

Safo Martin K, Abdulmalik Osheiza, Lin Hsiang Ru, Asakura Toshio, Abraham Donald J

Abstract excerpt

The crystal structures of R- and T-state hemoglobin (Hb) Bassett have been determined to 2.15 and 1.80 A resolution, respectively. Physiologically, Hb Bassett (alphaAsp94-->Ala) is characterized by a low affinity for oxygen, a reduced Bohr effect and low cooperativity, as well as being slightly unstable (compared with normal adult hemoglobin; HbA). Comparisons between the Hb Bassett structures and previously...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Hemoglobins

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

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 15681866
DOI: 10.1107/S0907444904030501

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

Structures of R- and T-state hemoglobin Bassett: elucidating the structural basis for the low oxygen affinity of a mutant hemoglobin.PMID 15681866Read ↗

Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity.Semantic proximity Read ↗

Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional characterization of a high oxygen affinity natural mutant.Semantic proximity Read ↗

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

Hemoglobin Saint Mandé [beta 102 (G4) Asn----Tyr]. Functional studies and structural modeling reveal an altered T state.Semantic proximity Read ↗

Novel hemoglobin (Hb Grey Lynn) substitution (alpha91Leu --> Phe) affects heme interactions and alpha1beta2 contacts.Semantic proximity Read ↗

Hb Santa Clara (beta 97His-->Asn), a human haemoglobin variant: functional characterization and structure modelling.Semantic proximity Read ↗

Hb Montfermeil [beta 130(H8) Tyr-->Cys]: suggests a key role for the interaction between helix A and H in oxygen affinity of the hemoglobin molecule.Semantic 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 ↗

Structure and function of hemoglobin variants at an internal hydrophobic site: consequences of mutations at the beta 27 (B9) position.Semantic proximity Read ↗

Hemoglobin Rothschild: Structural Rationalization of Decreased O <sub>2</sub> Affinity as a Consequence of a β37(C3)Trp→Arg MutationSemantic proximity Read ↗

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

Crystal structures of HbA2 and HbE and modeling of hemoglobin delta 4: interpretation of the thermal stability and the antisickling effect of HbA2 and identification of the ferrocyanide binding site in Hb.Semantic proximity Read ↗

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