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

Thermally denatured state determines refolding in lipase: mutational analysis.

Protein science : a publication of the Protein Society - 1 Jun 2009

Ahmad Shoeb, Rao Nalam Madhusudhana

Abstract excerpt

Irreversibility of thermally denatured proteins due to aggregation limits thermodynamic characterization of proteins and also confounds the identification of thermostable mutants in protein populations. Identification of mutations that prevent the aggregation of unfolded proteins provides insights into folding pathways. In a lipase from Bacillus subtilis, evolved by directed evolution procedures, the...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to DNA Mutational Analysis
Share to Hot Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipase

Share to Mutation

Share to Proline

Share to Protein Denaturation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 19472328
DOI: 10.1002/pro.126
PMCID: PMC2774429

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Thermally denatured state determines refolding in lipase: mutational analysis.PMID 19472328Read ↗

In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation.Semantic proximity Read ↗

Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight.Semantic proximity Read ↗

Understanding the thermostability and activity of Bacillus subtilis lipase mutants: insights from molecular dynamics simulations.Semantic proximity Read ↗

Stability curves of laboratory evolved thermostable mutants of a Bacillus subtilis lipase.Semantic proximity Read ↗

Structural determinants of cold adaptation and stability in a large protein.Semantic proximity Read ↗

Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.Semantic proximity Read ↗

Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin.Semantic proximity Read ↗

Engineering lipase A from mesophilic Bacillus subtilis for activity at low temperatures.Semantic proximity Read ↗

Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase.Semantic proximity Read ↗

Isolation of a thermostable variant of Lip2 lipase from Yarrowia lipolytica by directed evolution and deeper insight into the denaturation mechanisms involved.Semantic proximity Read ↗

Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase.Semantic proximity Read ↗

Glucose isomerase: insights into protein engineering for increased thermostability.Semantic proximity Read ↗

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