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

Surface and interface beta-chain residues synergistically affect hemoglobin assembly.

Biochemical and biophysical research communications - 21 Apr 2000

Yamaguchi T, Yang Y, McDonald M J, Adachi K

Abstract excerpt

Homo- and heterotetramer formations of beta112 variants (beta(112Cys-->Asp), beta(112Cys-->Ser), beta(112Cys-->Thr), and beta(112Cys-->Val)) of hemoglobin were characterized in the presence and absence of beta(16Gly-->Asp) in vitro. In all cases an alteration in overall surface charge (beta(16Gly-->Asp)) decreased the beta(4) homotetramer stability (association constants as determined by gel-permeation...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Genetic Variation
Share to Globins

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

Share to Hemoglobins

Share to Kinetics

Share to Macromolecular Substances

Share to Mutagenesis, Site-Directed

Share to Recombinant Proteins

Source

Identifiers

PMID: 10772884
DOI: 10.1006/bbrc.2000.2504

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

Surface and interface beta-chain residues synergistically affect hemoglobin assembly.PMID 10772884Read ↗

The heme-globin and dimerization equilibria of recombinant human hemoglobins carrying site-specific beta chains mutations.Semantic proximity Read ↗

Recombinant sickle hemoglobin containing a lysine substitution at Asp-85(alpha): expression in yeast, functional properties, and participation in gel formation.Semantic proximity Read ↗

Modification of axial fiber contact residues impact sickle hemoglobin polymerization by perturbing a network of coupled interactions.Semantic proximity Read ↗

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.Semantic proximity Read ↗

Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(beta) at the primary aggregation site substituted by Ala.Semantic proximity Read ↗

Mutation of interfaces in domain-swapped human betaB2-crystallin.Semantic proximity Read ↗

Distinct domain responses of R-state human hemoglobins A, C, and S to anions.Semantic proximity Read ↗

Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.Semantic proximity Read ↗

Structural, functional, and subunit assembly properties of hemoglobin Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site maturation at a critical C-terminal residue.Semantic proximity Read ↗

Linkage of interactions in sickle hemoglobin fiber assembly: inhibitory effect emanating from mutations in the AB region of the alpha-chain is annulled by a mutation at its EF corner.Semantic proximity Read ↗

Characteristic of aromatic amino acid substitution at alpha 96 of hemoglobin.Semantic proximity Read ↗

Influence of semisynthetic modification of the scaffold of a contact domain of HbS on polymerization: role of flexible surface topology in polymerization inhibition.Semantic proximity Read ↗

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