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

On the origin of the thermostabilization of proteins induced by sodium phosphate.

Journal of the American Chemical Society - 13 Jul 2005

Fayos Rosa, Pons Miquel, Millet Oscar

Abstract excerpt

The B1 domain of protein L shows a linear rise in thermostability with increasing concentrations of sodium phosphate. Equal behavior is observed for a set of mutant proteins where surface lysines are mutated to noncharged residues, but the mutant's thermostabilities show different sensitivities to phosphate, encoded in the varying slopes observed (mi). The melting temperature in the absence of the cosolute also...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to DNA-Binding Proteins
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Osmolar Concentration

Share to Phosphates

Share to Protein Denaturation

Share to Temperature

Source

Identifiers

PMID: 15998065
DOI: 10.1021/ja051352e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

On the origin of the thermostabilization of proteins induced by sodium phosphate.PMID 15998065Read ↗

Protein stabilization and the Hofmeister effect: the role of hydrophobic solvation.Semantic proximity Read ↗

An efficient method to predict protein thermostability in alanine mutation.Semantic proximity Read ↗

Thermodynamic effects of replacements of Pro residues in helix interiors of maltose-binding protein.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 ↗

Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values.Semantic proximity Read ↗

pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability.Semantic proximity Read ↗

Proteins under extreme physical conditions.Semantic proximity Read ↗

Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase.Semantic proximity Read ↗

Increasing the hydrophobic interaction between terminal W-motifs enhances the stability of Salmonella typhimurium sialidase. A general strategy for the stabilization of beta-propeller protein fold.Semantic proximity Read ↗

Type I 'antifreeze' proteins. Structure-activity studies and mechanisms of ice growth inhibition.Semantic proximity Read ↗

Mechanisms of protein-ligand association and its modulation by protein mutations.Semantic proximity Read ↗

Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease.Semantic proximity Read ↗

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