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 structure of an engineered biologically potent insulin monomer, B16 Tyr-->His, as determined by nuclear magnetic resonance spectroscopy.

Biochemistry - 5 Jul 1994

Ludvigsen S, Roy M, Thøgersen H, Kaarsholm N C

Abstract excerpt

Site-directed mutagenesis is used in conjunction with 1H nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy in order to find an insulin species amenable for structure determination in aqueous solution by NMR spectroscopy. A successful candidate in this respect, i.e., B16 Tyr-->His mutant insulin, is identified and selected for detailed characterization by two-dimensional 1H NMR. This mutant...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Computer Simulation

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

Share to Hydrogen-Ion Concentration

Share to Insulin

Share to Magnetic Resonance Spectroscopy

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 8025104
DOI: 10.1021/bi00192a003

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 structure of an engineered biologically potent insulin monomer, B16 Tyr-->His, as determined by nuclear magnetic resonance spectroscopy.PMID 8025104Read ↗

Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native 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 ↗

1H NMR spectrum of the native human insulin monomer. Evidence for conformational differences between the monomer and aggregated forms.Semantic proximity Read ↗

Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus.Semantic proximity Read ↗

The road to the first, fully active and more stable human insulin variant with an additional disulfide bond.Semantic proximity Read ↗

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

Non-standard insulin design: structure-activity relationships at the periphery of the insulin receptor.Semantic proximity Read ↗

Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex.Semantic proximity Read ↗

A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure.Semantic proximity Read ↗

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

A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.Semantic proximity Read ↗

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

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