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

Exploring the charge space of protein-protein association: a proteomic study.

Proteins - 15 Aug 2005

Shaul Yossi, Schreiber Gideon

Abstract excerpt

The rate of association of a protein complex is a function of an intrinsic basal rate and of the magnitude of electrostatic steering. In the present study we analyze the contribution of electrostatics towards the association rate of proteins in a database of 68 transient hetero-protein-protein complexes. Our calculations are based on an upgraded version of the computer algorithm PARE, which was shown to...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Biophysical Phenomena
Share to Biophysics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Databases, Protein

Share to Protein Folding

Share to Protein Interaction Mapping

Share to Proteomics

Share to Static Electricity

Source

Identifiers

PMID: 15887221
DOI: 10.1002/prot.20489

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

Exploring the charge space of protein-protein association: a proteomic study.PMID 15887221Read ↗

Electrostatic design of protein-protein association rates.Semantic proximity Read ↗

AESOP: A Python Library for Investigating Electrostatics in Protein Interactions.Semantic proximity Read ↗

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

Inferring the microscopic surface energy of protein-protein interfaces from mutation data.Semantic proximity Read ↗

Rational design of faster associating and tighter binding protein complexes.Semantic proximity Read ↗

SSIPe: accurately estimating protein-protein binding affinity change upon mutations using evolutionary profiles in combination with an optimized physical energy function.Semantic proximity Read ↗

Rapid, electrostatically assisted association of proteins.Semantic proximity Read ↗

Prediction of protein-protein association rates from a transition-state theory.Semantic proximity Read ↗

Characterizing changes in the rate of protein-protein dissociation upon interface mutation using hotspot energy and organization.Semantic proximity Read ↗

BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations.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 ↗

Modeling effects of human single nucleotide polymorphisms on protein-protein interactions.Semantic proximity Read ↗

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