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 characteristics of an abnormal protein influencing its proteolytic susceptibility.

Journal of biotechnology - 1 Apr 1992

Kosinski M J, Bailey J E

Abstract excerpt

Structural properties of two similar beta-galactosidase fragments were investigated to determine how they influence the fragments' degradation rate in Escherichia coli. Both fragments resulting from a C-terminal nonsense mutation in lacZ, the CSH11 polypeptide and its 90 kDa degradative intermediate, exist predominantly as monomer subunits instead of in the tetrameric form characteristic of the native enzyme....

Topics

Blotting, Western
Chromatography, Affinity
Chymotrypsin
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Mutation
Peptide Fragments
Protein Denaturation
Temperature
beta-Galactosidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 1368059
DOI: 10.1016/0168-1656(92)90093-o

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1368059-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural characteristics of an abnormal protein influencing its proteolytic susceptibility.PMID 1368059Read ↗

Proteolytic response to the expression of an abnormal beta-galactosidase in Escherichia coli.Semantic proximity Read ↗

Temperature and induction effects on the degradation rate of an abnormal beta-galactosidase in Escherichia coli.Semantic proximity Read ↗

The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.Semantic proximity Read ↗

Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.Semantic proximity Read ↗

Assessing genetic stability of a recombinant protein at the nucleic acid level.Semantic proximity Read ↗

Accommodation of single amino acid insertions by the native state of staphylococcal nuclease.Semantic proximity Read ↗

The atomic model of the human protective protein/cathepsin A suggests a structural basis for galactosialidosis.Semantic proximity Read ↗

Molecular basis for zymogen-like autoinhibition of the M60-like metallopeptidase YghJSemantic proximity Read ↗

Molecular properties of the glucosaminidase AcmA from Lactococcus lactis MG1363: mutational and biochemical analyses.Semantic proximity Read ↗

Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.Semantic proximity Read ↗

Carboxy-terminal determinants of intracellular protein degradation.Semantic proximity Read ↗

Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation.Semantic proximity Read ↗

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