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

Conformational stabilities of the rat alpha- and beta-parvalbumins.

FEBS letters - 15 Jan 1999

Henzl M T, Graham J S

Abstract excerpt

It is widely believed that beta-parvalbumin (PV) isoforms are intrinsically less stable than alpha-parvalbumins, due to greater electrostatic repulsion and an abbreviated C-terminal helix. However, when examined by differential scanning calorimetry, the apo-form of the rat beta-PV (i.e. oncomodulin) actually displays greater thermal stability than the alpha-PV. Whereas the melting temperature of the a isoform is...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Hydrogen-Ion Concentration
Share to Models, Molecular

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

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Temperature

Source

Identifiers

PMID: 9929009
DOI: 10.1016/s0014-5793(98)01666-4

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 · 10 closest

Conformational stabilities of the rat alpha- and beta-parvalbumins.PMID 9929009Read ↗

Disparate impact of the S33V mutation on conformational stability in rat β-parvalbumin (oncomodulin) and chicken parvalbumin 3.Semantic proximity Read ↗

Impact of proline residues on parvalbumin stability.Semantic proximity Read ↗

Leucine 85 is an important determinant of divalent ion affinity in rat beta-parvalbumin (Oncomodulin).Semantic proximity Read ↗

Remodeling of the AB site of rat parvalbumin and oncomodulin into a canonical EF-hand.Semantic proximity Read ↗

Comprehensive analysis of the roles of 'black' and 'gray' clusters in structure and function of rat β-parvalbumin.Semantic proximity Read ↗

Stability, activity and flexibility in alpha-lactalbumin.Semantic proximity Read ↗

Stability of monomeric Cro variants: Isoenergetic transformation of a type I' to a type II' beta-hairpin by single amino acid replacements.Semantic proximity Read ↗

Effects of metal binding affinity on the chemical and thermal stability of site-directed mutants of rat oncomodulin.Semantic proximity Read ↗

Comparison of metal ion-induced conformational changes in parvalbumin and oncomodulin as probed by the intrinsic fluorescence of tryptophan 102.Semantic proximity Read ↗

Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity.Semantic proximity Read ↗

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