Thermodynamics

All in One: Cavity Detection, Druggability Estimate, Cavity-Based Pharmacophore Perception, and Virtual Screening

Discovering the very first ligands of pharmacologically important targets in a fast and cost-efficient manner is an important issue in drug discovery.

Tran-Nguyen, V.

• Jan 28, 2019 • 1 min read

Alleles

Recovery of known T-cell epitopes by computational scanning of a viral genome.

A new computational method (EpiDock) is proposed for predicting peptide binding to class I MHC proteins, from the amino acid sequence of any protein of immunological interest.

Logean, A.

• Apr 1, 2002 • 1 min read

Base Sequence

Thermodynamic stability of HLA-B*2705. Peptide complexes. Effect of peptide and major histocompatibility complex protein mutations.

Designing synthetic vaccines from class I major histocompatibility complex (MHC)-binding antigenic peptides requires not only knowledge of the binding affinity of the designed …

Dédier, S.

• Sep 1, 2000 • 1 min read

Amino Acid Sequence

Fine specificity of antigen binding to two class I major histocompatibility proteins (B2705 and B2703) differing in a single amino acid residue.

Starting from the X-ray structure of a class I major histocompatibility complex (MHC)-encoded protein (HLA-B*2705), a naturally presented self-nonapeptide and two synthetic …

Rognan, D.

• Sep 1, 1997 • 1 min read

All in One: Cavity Detection, Druggability Estimate, Cavity-Based Pharmacophore Perception, and Virtual Screening

Recovery of known T-cell epitopes by computational scanning of a viral genome.

Thermodynamic stability of HLA-B*2705. Peptide complexes. Effect of peptide and major histocompatibility complex protein mutations.

Fine specificity of antigen binding to two class I major histocompatibility proteins (B*2705 and B*2703) differing in a single amino acid residue.

Fine specificity of antigen binding to two class I major histocompatibility proteins (B2705 and B2703) differing in a single amino acid residue.