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

Metal binding properties of recombinant rat parvalbumin wild-type and F102W mutant.

The Journal of biological chemistry - 5 Oct 1993

Pauls T L, Durussel I, Cox J A, Clark I D, Szabo A G, Gagné S M, Sykes B D, Berchtold M W

Abstract excerpt

Rat parvalbumin (PV), an EF-hand type Ca(2+)-binding protein, was expressed in Escherichia coli and mutated by replacing a Phe at position 102 with a unique Trp in order to introduce a distinct fluorescent label into the protein. Mass spectroscopy and NMR data indicate that the recombinant wild-type (PVWT) and F102W mutant (PVF102W) proteins have the expected molecular weight and retain the native structure. Both...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Calcium
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Oligodeoxyribonucleotides

Share to Recombinant Proteins

Source

Identifiers

PMID: 8407923

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 · 11 closest

Metal binding properties of recombinant rat parvalbumin wild-type and F102W mutant.PMID 8407923Read ↗

Human recombinant alpha-parvalbumin and nine mutants with individually inactivated calcium- and magnesium-binding sites: biochemical and immunological properties.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 ↗

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

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

Structure-fluorescence correlations in a single tryptophan mutant of carp parvalbumin: solution structure, backbone and side-chain dynamics.Semantic proximity Read ↗

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

Molecular mechanisms of calcium and magnesium binding to parvalbumin.Semantic proximity Read ↗

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

Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins.Semantic proximity Read ↗

Biophysical studies of engineered mutant proteins based on calbindin D9k modified in the pseudo EF-hand.Semantic proximity Read ↗

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