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

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

The journal of physical chemistry. B - 16 Dec 2010

Tan Anmin, Markus Lindsey A, Henzl Michael T

Abstract excerpt

Rat β-parvalbumin (β-PV) and chicken parvalbumin 3 (CPV3) exhibit diminished Ca(2+) affinity. Their sequences, 70% identical, are unusual in that serine replaces the consensus residue, valine, at position 33. Reasoning that the substitution of a compact, polar hydroxymethyl moiety for a bulky, apolar isopropyl group might contribute to the attenuated Ca(2+) affinities, we have characterized the S33V variants of...

Read the complete abstract on PubMed

Topics

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

Share to Protein Stability
Share to Calcium-Binding Proteins

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

Share to Chickens

Share to Circular Dichroism

Share to Parvalbumins

Share to Protein Conformation

Share to Sequence Alignment

Share to Temperature

Source

Identifiers

PMID: 20961100
DOI: 10.1021/jp1063325

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

Disparate impact of the S33V mutation on conformational stability in rat β-parvalbumin (oncomodulin) and chicken parvalbumin 3.PMID 20961100Read ↗

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

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

Conformational stabilities of the rat alpha- and beta-parvalbumins.Semantic proximity Read ↗

Structural determinants of calcium binding beyond the EF-hand binding site: a study of alpha parvalbuminsSemantic proximity Read ↗

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

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

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

Electrospray ionization mass spectrometry: analysis of the Ca2+-binding properties of human recombinant alpha-parvalbumin and nine mutant proteins.Semantic proximity Read ↗

A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.Semantic proximity Read ↗

Site-specific replacement of amino acid residues within the CD binding loop of rat oncomodulin.Semantic proximity Read ↗

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

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