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

Molecular dynamics force probe simulations of antibody/antigen unbinding: entropic control and nonadditivity of unbinding forces.

Biophysical journal - 1 Sept 2001

Heymann B, Grubmüller H

Abstract excerpt

Unbinding of a spin-labeled dinitrophenyl (DNP) hapten from the monoclonal antibody AN02 F(ab) fragment has been studied by force probe molecular dynamics (FPMD) simulations. In our nanosecond simulations, unbinding was enforced by pulling the hapten molecule out of the binding pocket. Detailed inspection of the FPMD trajectories revealed a large heterogeneity of enforced unbinding pathways and a correspondingly...

Read the complete abstract on PubMed

Topics

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

Share to Antigen-Antibody Complex
Share to Entropy
Share to Haptens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulin Heavy Chains

Share to Immunoglobulin Light Chains

Share to Solvents

Share to Spin Labels

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 11509346
DOI: 10.1016/S0006-3495(01)75787-6
PMCID: PMC1301611

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 · 8 closest

Molecular dynamics force probe simulations of antibody/antigen unbinding: entropic control and nonadditivity of unbinding forces.PMID 11509346Read ↗

Improving Prediction Accuracy of Binding Free Energies and Poses of HIV Integrase Complexes Using the Binding Energy Distribution Analysis Method with Flattening Potentials.Semantic proximity Read ↗

A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex.Semantic proximity Read ↗

Characterization of monobody scaffold interactions with ligand via force spectroscopy and steered molecular dynamics.Semantic proximity Read ↗

Mutations in Antibody Fragments Modulate Allosteric Response Via Hydrogen-Bond Network Fluctuations.Semantic proximity Read ↗

Determination of the differential effects of hydrogen bonding and water release on the binding of FK506 to native and Tyr82-->Phe82 FKBP-12 proteins using free energy simulations.Semantic proximity Read ↗

Molecular simulations of multimodal ligand-protein binding: elucidation of binding sites and correlation with experiments.Semantic proximity Read ↗

Computer modeling of electrostatic steering and orientational effects in antibody-antigen association.Semantic proximity Read ↗

Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.Semantic proximity Read ↗

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