Oxidative folding of human lysozyme: effects of the loss of two disulfide bonds and the introduction of a calcium-binding site.

doi:10.1023/a:1010997500932

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

Back to search

Article

Oxidative folding of human lysozyme: effects of the loss of two disulfide bonds and the introduction of a calcium-binding site.

Journal of protein chemistry - 1 May 2001

Kurokawa Y, Koganesawa N, Kobashigawa Y, Koshiba T, Demura M, Niita K

Abstract excerpt

Mutant human lysozymes (HLZ) lacking two disulfide bonds were constructed to study the importance of each disulfide bond on oxidative refolding. To avoid destabilization, a calcium-binding site was introduced. Five of the six species of two-disulfide mutants could be obtained with enzymatic activity. Based on the information obtained from refolding and unfolding experiments, the order of importance in oxidative...

Topics

Binding Sites
Calcium
Circular Dichroism
Disulfides
Hot Temperature
Humans
Muramidase
Mutagenesis, Site-Directed
Mutation
Oxidation-Reduction
Protein Conformation
Protein Folding
Structure-Activity Relationship
Thioredoxins

Source

Open in PubMed

Identifiers

PMID: 11594463
DOI: 10.1023/a:1010997500932

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

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

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics