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

Mechanisms of protein-ligand association and its modulation by protein mutations.

Biophysical journal - 2 Feb 2011

Held Martin, Metzner Philipp, Prinz Jan-Hendrik, Noé Frank

Abstract excerpt

Protein-ligand interactions are essential for nearly all biological processes, and yet the biophysical mechanism that enables potential binding partners to associate before specific binding occurs remains poorly understood. Fundamental questions include which factors influence the formation of protein-ligand encounter complexes, and whether designated association pathways exist. To address these questions, we...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli Proteins
Share to Kinetics
Share to Ligands

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

Share to Models, Molecular

Share to Mutant Proteins

Share to Mutation

Share to Phosphate-Binding Proteins

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 21281585
DOI: 10.1016/j.bpj.2010.12.3699
PMCID: PMC3030248

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

Mechanisms of protein-ligand association and its modulation by protein mutations.PMID 21281585Read ↗

Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.Semantic proximity Read ↗

Exploring the charge space of protein-protein association: a proteomic study.Semantic proximity Read ↗

Implementing and Assessing an Alchemical Method for Calculating Protein-Protein Binding Free Energy.Semantic proximity Read ↗

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

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

Double Mutant Cycles as a Tool to Address Folding, Binding, and Allostery.Semantic proximity Read ↗

Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMDSemantic proximity Read ↗

Transition states and the meaning of Phi-values in protein folding kinetics.Semantic proximity Read ↗

Relative Binding Free Energy Estimation of Congeneric Ligands and Macromolecular Mutants with the Alchemical Transfer Method with Coordinate Swapping.Semantic proximity Read ↗

Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMD.Semantic proximity Read ↗

Mutations as trapdoors to two competing native conformations of the Rop-dimer.Semantic proximity Read ↗

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