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

High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,.

Biochemistry - 31 Mar 1998

Kavanaugh J S, Weydert J A, Rogers P H, Arnone A

Abstract excerpt

The high-resolution X-ray structures of the deoxy forms of four recombinant hemoglobins in which Trp37(C3)beta is replaced with Tyr (betaW37Y), Ala (betaW37A), Glu (betaW37E), or Gly (betaW37G) have been refined and analyzed with superposition methods that partition mutation-induced perturbations into quaternary structure changes and tertiary structure changes. In addition, a new cross-validation statistic that...

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 Crystallography, X-Ray

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

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Reproducibility of Results

Share to Tryptophan

Source

Identifiers

PMID: 9521756
DOI: 10.1021/bi9708702

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

High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,.PMID 9521756Read ↗

Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions.Semantic proximity Read ↗

Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37 beta and 145 beta mutations.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 ↗

Thermodynamic studies on the equilibrium properties of a series of recombinant betaW37 hemoglobin mutants.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 ↗

Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: evidence for high-affinity T quaternary structures.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 ↗

Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.Semantic proximity Read ↗

A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.Semantic proximity Read ↗

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

Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding: a study of mutants at alpha 42, alpha 140, beta 145 tyrosine or beta 37 tryptophan.Semantic proximity Read ↗

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