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

Recombinant hemoglobins with low oxygen affinity and high cooperativity.

Biophysical chemistry - 10 Jul 2002

Tsai Ching-Hsuan, Ho Chien

Abstract excerpt

By introducing an additional H-bond in the alpha(1)beta(2) subunit interface or altering the charge properties of the amino acid residues in the alpha(1)beta(1) subunit interface of the hemoglobin molecule, we have designed and expressed recombinant hemoglobins (rHbs) with low oxygen affinity and high cooperativity. Oxygen-binding measurements of these rHbs under various experimental conditions show interesting...

Read the complete abstract on PubMed

Topics

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

Share to Oxygen
Share to Hemoglobins
Share to Kinetics

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

Share to Mutation

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protons

Share to Recombinant Proteins

Share to Temperature

Source

Identifiers

PMID: 12128186
DOI: 10.1016/s0301-4622(02)00081-9

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

Recombinant hemoglobins with low oxygen affinity and high cooperativity.PMID 12128186Read ↗

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

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

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

Oxygen binding and other physical properties of human hemoglobin made in yeast.Semantic proximity Read ↗

Quaternary structure of carbonmonoxyhemoglobins in solution: structural changes induced by the allosteric effector inositol hexaphosphate.Semantic proximity Read ↗

COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000.Semantic proximity Read ↗

An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.Semantic proximity Read ↗

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

Molecular code for cooperativity in hemoglobin.Semantic proximity Read ↗

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

Probing the conformation of hemoglobin presbyterian in the R-state.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 ↗

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