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

Free energy simulations of the HyHEL-10/HEL antibody-antigen complex.

Protein engineering - 1 Jul 1995

Pomès R, Willson R C, McCammon J A

Abstract excerpt

Free energy simulations are reported for the N31LD mutation, both in the HyHEL-10-HEL antibody-lysozyme complex and in the unliganded antibody, using the thermodynamic-cycle perturbation method. The present study suggests that the mutation would change the free energy of binding of the complex by -5.6 kcal/mol (unrestrained free energy simulations), by -0.5 kcal/mol (free energy simulations with a restrained...

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 Immunoglobulin Variable Region
Share to Models, Chemical

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

Share to Muramidase

Share to Mutation

Share to Protein Conformation

Share to Thermodynamics

Source

Identifiers

PMID: 8577695
DOI: 10.1093/protein/8.7.663

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

Free energy simulations of the HyHEL-10/HEL antibody-antigen complex.PMID 8577695Read ↗

Thermodynamics of antibody-antigen interaction revealed by mutation analysis of antibody variable regions.Semantic proximity Read ↗

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

Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL.Semantic proximity Read ↗

Association energetics of cross-reactive and specific antibodies.Semantic proximity Read ↗

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

Light chain somatic mutations change thermodynamics of binding and water coordination in the HyHEL-10 family of antibodies.Semantic proximity Read ↗

pH dependence of antibody/lysozyme complexation.Semantic proximity Read ↗

Assessment of Mutational Effects on Peptide Stability through Confinement Simulations.Semantic proximity Read ↗

Analysis of protein-protein interactions and the effects of amino acid mutations on their energetics. The importance of water molecules in the binding epitope.Semantic proximity Read ↗

Single mutation induced H3N2 hemagglutinin antibody neutralization: a free energy perturbation study.Semantic proximity Read ↗

Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes.Semantic proximity Read ↗

Thermodynamic consequences of grafting enhanced affinity toward the mutated antigen onto an antibody. The case of anti-lysozyme antibody, HyHEL-10.Semantic proximity Read ↗

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