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

Importance of a potential salt bridge and hydrophobic core in the function and oligomerization of a small heat shock protein.

Protein and peptide letters - 1 Jun 2010

Wen Z, Wang Y, Xu X, Yang B, Li W, Xie M

Abstract excerpt

SsHSP14.1, a novel sHSP from the hyper-thermophilic archaeon Sulfolobus solfataricus (S. solfataricus), is reported herein to function to protect EcoR I from heat-induced inactivation. A predicted salt bridge and hydrophobic interactions were found to be important for this function.

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 Deoxyribonuclease EcoRI
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hot Temperature

Share to Hydrophobic and Hydrophilic Interactions

Share to Protein Multimerization

Share to Sodium Chloride

Share to Sulfolobus solfataricus

Source

Identifiers

PMID: 20015024
DOI: 10.2174/092986610791190273

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

Importance of a potential salt bridge and hydrophobic core in the function and oligomerization of a small heat shock protein.PMID 20015024Read ↗

Molecular chaperone function of three small heat-shock proteins from a model probiotic speciesSemantic proximity Read ↗

Multiple oligomeric structures of a bacterial small heat shock protein.Semantic proximity Read ↗

Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.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 ↗

The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions.Semantic proximity Read ↗

Small heat shock proteins and protein-misfolding diseases.Semantic proximity Read ↗

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

Replacement of Arg in the conserved N-terminal RLFDQxFG motif affects physico-chemical properties and chaperone-like activity of human small heat shock protein HspB8 (Hsp22).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 ↗

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

Substrate binding site flexibility of the small heat shock protein molecular chaperones.Semantic proximity Read ↗

Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” statesSemantic proximity Read ↗

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