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

A sedimentation equilibrium study of platypus insulin: the HB10D mutant does not associate beyond dimer.

Biophysical chemistry - 30 Mar 1998

Nourse A, Jeffrey P D

Abstract excerpt

An extensive study of the self-association patterns of zinc-free synthetic native and mutant (HB10D) platypus insulin in solution (pH = 7.0; I = 0.1 M; 25 degrees C) has been undertaken using the method of sedimentation equilibrium. The data was fitted to a mathematical equation describing the indefinite duoisodesmic (IDI) model of self-association [A.E. Mark, P.D. Jeffrey, Biol. Chem. Hoppe-Slayer, 371 (1990)...

Read the complete abstract on PubMed

Topics

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

Share to Cattle
Share to Insulin
Share to Models, Chemical

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

Share to Molecular Weight

Share to Mutation

Share to Thermodynamics

Share to Ultracentrifugation

Source

Identifiers

PMID: 9591358
DOI: 10.1016/s0301-4622(97)00131-2

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A sedimentation equilibrium study of platypus insulin: the HB10D mutant does not associate beyond dimer.PMID 9591358Read ↗

Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions.Semantic proximity Read ↗

Application of SIMSTEX to oligomerization of insulin analogs and mutants.Semantic proximity Read ↗

A Conserved Histidine in Insulin Is Required for the Foldability of Human ProinsulinSemantic proximity Read ↗

Altered ionization of the B13 Glu in insulin B9 and B10 mutants: a computational analysis.Semantic proximity Read ↗

Prediction of the association state of insulin using spectral parameters.Semantic proximity Read ↗

Changes in secondary structure follow the dissociation of human insulin hexamers: a circular dichroism study.Semantic proximity Read ↗

Probing the mechanism of insulin fibril formation with insulin mutants.Semantic proximity Read ↗

Role of B13 Glu in insulin assembly. The hexamer structure of recombinant mutant (B13 Glu-->Gln) insulin.Semantic proximity Read ↗

Role of disulfide bonds in the structure and activity of human insulin.Semantic proximity Read ↗

Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant: elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin.Semantic proximity Read ↗

Mutation of active site residues of insulin-degrading enzyme alters allosteric interactions.Semantic proximity Read ↗

The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.Semantic proximity Read ↗

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