Crystallography

Predicting binding affinities of protein ligands from three-dimensional models: application to peptide binding to class I major histocompatibility proteins.

A simple and fast free energy scoring function (Fresno) has been developed to predict the binding free energy of peptides to class I major histocompatibility (MHC) proteins.

Rognan, D.

• Nov 1, 1999 • 1 min read

Substituting nonpeptidic spacers for the T cell receptor-binding part of class I major histocompatibility complex-binding peptides.

X-ray diffraction studies as well as structure-activity relationships indicate that the central part of class I major histocompatibility complex (MHC)-binding nonapeptides …

Krebs, S.

• Jul 1, 1998 • 1 min read

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

Predicting binding affinities of protein ligands from three-dimensional models: application to peptide binding to class I major histocompatibility proteins.

Substituting nonpeptidic spacers for the T cell receptor-binding part of class I major histocompatibility complex-binding peptides.

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.