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

Thermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.

PloS one - 1 Jan 2014

Srivastava Ashutosh, Sinha Somdatta

Abstract excerpt

Proteins in thermophilic organisms remain stable and function optimally at high temperatures. Owing to their important applicability in many industrial processes, such thermostable proteins have been studied extensively, and several structural factors attributed to their enhanced stability. How these factors render the emergent property of thermostability to proteins, even in situations where no significant...

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 Bacterial Proteins
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hot Temperature

Share to Molecular Dynamics Simulation

Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Sterol Esterase

Source

Open in PubMed Open full text

Identifiers

PMID: 25122499
DOI: 10.1371/journal.pone.0102856
PMCID: PMC4133394

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

Thermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.PMID 25122499Read ↗

Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.Semantic proximity Read ↗

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

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

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

Thermostabilizing mutations preferentially occur at structural weak spots with a high mutation ratio.Semantic proximity Read ↗

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

Insights of conformational dynamics on catalytic activity in the computational stability design of Bacillus subtilis LipA.Semantic proximity Read ↗

Integrating Sequence, Structure, and Graph-based Features for Elucidating the Stability of Thermophilic Proteins.Semantic proximity Read ↗

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

Turning a mesophilic protein into a thermophilic one: a computational approach based on 3D structural features.Semantic proximity Read ↗

Hook loop dynamics engineering transcended the barrier of activity-stability trade-off and boosted the thermostability of enzymes.Semantic proximity Read ↗

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

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