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

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

PloS one - 1 Jan 2012

Chan Chi-Ho, Wilbanks Cecily C, Makhatadze George I, Wong Kam-Bo

Abstract excerpt

Optimization of the surface charges is a promising strategy for increasing thermostability of proteins. Electrostatic contribution of ionizable groups to the protein stability can be estimated from the differences between the pKa values in the folded and unfolded states of a protein. Using this pKa-shift approach, we experimentally measured the electrostatic contribution of all aspartate and glutamate residues to...

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 Aspartic Acid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Benchmarking

Share to Glutamic Acid

Share to Protein Unfolding

Share to Ribosomal Proteins

Share to Static Electricity

Share to Surface Properties

Source

Open in PubMed Open full text

Identifiers

PMID: 22279578
DOI: 10.1371/journal.pone.0030296
PMCID: PMC3261180

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values.PMID 22279578Read ↗

Effects of charge-to-alanine substitutions on the stability of ribosomal protein L30e from Thermococcus celer.Semantic proximity Read ↗

Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e.Semantic proximity Read ↗

Empirical prediction of protein pKa values with residue mutation.Semantic proximity Read ↗

A pH-dependent computational approach to the effect of mutations on protein stability.Semantic proximity Read ↗

Toward accurate prediction of pKa values for internal protein residues: the importance of conformational relaxation and desolvation energy.Semantic proximity Read ↗

Alchemical Calculation of Relative Free Energies for Charge-Changing Mutations at Protein-Protein Interfaces Considering Fixed and Variable Protonation States.Semantic proximity Read ↗

Protein stability prediction: a Poisson-Boltzmann approach.Semantic proximity Read ↗

Protein electrostatics and pKa blind predictions; contribution from empirical predictions of internal ionizable residues.Semantic proximity Read ↗

pH and Charged Mutations Modulate Cold Shock Protein Folding and Stability: A Constant pH Monte Carlo Study.Semantic proximity Read ↗

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.Semantic proximity Read ↗

Charge Interactions in a Highly Charge-Depleted Protein.Semantic proximity Read ↗

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

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