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

Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin.

Proteins - 15 May 2006

Yamada Yoshiteru, Nakagawa Kanako, Yajima Takeo, Saito Keiko, Tokushima Akihito, Fujiwara Kazuo, Ikeguchi Masamichi

Abstract excerpt

A disulfide bond between cysteine 66 and cysteine 160 of equine beta-lactoglobulin was removed by substituting cysteine residues with alanine. This disulfide bond is conserved across the lipocalin family. The conformation and stability of the disulfide-deleted mutant protein was investigated by circular dichroism. The mutant protein assumes a native-like structure under physiological conditions and assumes a...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Horses

Share to Lactoglobulins

Share to Mutation

Share to Protein Denaturation

Share to Thermodynamics

Source

Identifiers

PMID: 16463267
DOI: 10.1002/prot.20905

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin.PMID 16463267Read ↗

Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography.Semantic proximity Read ↗

Unusual effects of an engineered disulfide on global and local protein stability.Semantic proximity Read ↗

Propensities for the formation of individual disulfide bonds in hen lysozyme and in the size and stability of disulfide-associated submolecular structures.Semantic proximity Read ↗

Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.Semantic proximity Read ↗

Analyses of native disulfide bond formations in the early stage of the folding process in mutant lysozymes where the long-range interactions in the denatured state were modulated.Semantic proximity Read ↗

Construction and characterization of beta-lactoglobulin chimeras.Semantic proximity Read ↗

Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.Semantic proximity Read ↗

Effect of amino acid substitutions at the subunit interface on the stability and aggregation properties of a dimeric protein: role of Arg 178 and Arg 218 at the Dimer interface of thymidylate synthase.Semantic proximity Read ↗

Stabilization of an Immunoglobulin Fold Domain by an Engineered Disulfide Bond at the Buried Hydrophobic RegionSemantic proximity Read ↗

Engineering nutritious proteins: improvement of stability in the designer protein MB-1 via introduction of disulfide bridges.Semantic proximity Read ↗

Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme.Semantic proximity Read ↗

Structure, stability and biological properties of a N-terminally truncated form of recombinant human interleukin-6 containing a single disulfide bond.Semantic proximity Read ↗

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