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

Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b.

Archives of biochemistry and biophysics - 1 Jan 2009

Fang Xianyang, Feng Yingang, Wang Jinfeng

Abstract excerpt

The role of residue K97 at the C-terminal end of archaeal [P62A]Ssh10b in the hyperthermostability of the protein is investigated using three K97-mutant variants: K97E-, K97A-, and DeltaK97-mutant [P62A]Ssh10b. The thermal- and GdmHCl-induced denaturation of the three mutant variants has been monitored by circular dichroism. The results reveal that the K97E mutation leads to a stronger destabilization effect than...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Models, Molecular

Share to Protein Conformation

Share to Protein Folding

Share to Static Electricity

Share to Thermodynamics

Source

Identifiers

PMID: 18851941
DOI: 10.1016/j.abb.2008.08.025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b.PMID 18851941Read ↗

A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b.Semantic proximity Read ↗

Salt bridges in the hyperthermophilic protein Ssh10b are resilient to temperature increases.Semantic proximity Read ↗

A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power.Semantic proximity Read ↗

Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization.Semantic proximity Read ↗

Reduction of salt-requirement of halophilic nucleoside diphosphate kinase by engineering S-S bond.Semantic proximity Read ↗

Increase of salt dependence of halophilic nucleoside diphosphate kinase caused by a single amino acid substitution.Semantic proximity Read ↗

Structural and dynamic effects of alpha-helix deletion in Sso7d: implications for protein thermal stability.Semantic proximity Read ↗

Effect of the Lys62Ala Mutation on the Thermal Stability of BstHPr Protein by Molecular Dynamics.Semantic proximity Read ↗

Thermal stability and unfolding pathways of Sso7d and its mutant F31A: insight from molecular dynamics simulation.Semantic proximity Read ↗

Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus.Semantic proximity Read ↗

Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events.Semantic proximity Read ↗

Engineering Clostridium absonum 7α-hydroxysteroid Dehydrogenase for Enhancing Thermostability Based on Flexible Site and ΔΔG Prediction.Semantic proximity Read ↗

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