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

Differences in aggregation properties of three site-specific mutants of recombinant human stefin B.

Protein science : a publication of the Protein Society - 1 Jan 2004

Kenig Manca, Berbić Selma, Krijestorac Aida, Kroon-Zitko Louise, Tusek Magda, Pompe-Novak Marusa, Zerovnik Eva

Abstract excerpt

We describe expression, purification, and characterization of three site-specific mutants of recombinant human stefin B: H75W, P36G, and P79S. The far- and near-UV CD spectra have shown that they have similar secondary and tertiary structures to the parent protein. The elution on gel-filtration suggests that recombinant human stefin B and the P36G variant are predominantly monomers, whereas the P79S variant is a...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, Ion Exchange

Share to Circular Dichroism

Share to Cystatins

Share to Databases, Factual

Share to Fluorescent Dyes

Source

Open in PubMed Open full text

Identifiers

PMID: 14691222
DOI: 10.1110/ps.03270904
PMCID: PMC2286520

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 · 12 closest

Differences in aggregation properties of three site-specific mutants of recombinant human stefin B.PMID 14691222Read ↗

The cross-road between the mechanisms of protein folding and aggregation; study of human stefin B and its H75W mutant.Semantic proximity Read ↗

High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation.Semantic proximity Read ↗

Human stefin B: from its structure, folding, and aggregation to its function in health and diseaseSemantic proximity Read ↗

Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.Semantic proximity Read ↗

Structure-function studies of an engineered scaffold protein derived from Stefin A. II: Development and applications of the SQT variant.Semantic proximity Read ↗

Essential role of proline isomerization in stefin B tetramer formation.Semantic proximity Read ↗

Structure-function studies of an engineered scaffold protein derived from stefin A. I: Development of the SQM variant.Semantic proximity Read ↗

Mutations in the QVVAG region of the cysteine proteinase inhibitor stefin B.Semantic proximity Read ↗

Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain.Semantic proximity Read ↗

Effect of amino acid variations in the central region of human serum amyloid A on the amyloidogenic properties.Semantic proximity Read ↗

Mouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain-like endo- and exopeptidases.Semantic proximity Read ↗

Structural and folding dynamic properties of the T70N variant of human lysozyme.Semantic proximity Read ↗

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