Folkers, G.

A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions.

Oligopeptides that interact with oxoanions were developed by rational design methods.

Demuth, C.

Use of fluorescence polarization to monitor MHC-peptide interactions in solution.

We describe here fluorescence polarization-based methods to investigate class I MHC-peptide interactions in solution.

Dédier, S.

NMR-restrained docking of a peptidic inhibitor to the N-terminal domain of the phosphoenolpyruvate:sugar phosphotransferase enzyme I.

Starting from the NMR structure of the binary complex between the N-terminal domain of the unphosphorylated enzyme I (EIN) of the phosphoenolpyruvate:sugar phosphotransferase (PTS) …

Rognan, D.

Protein-Based Virtual Screening of Chemical Databases. 1. Evaluation of Different Docking/Scoring Combinations

Three different database docking programs (Dock, FlexX, Gold) have been used in combination with seven scoring functions (Chemscore, Dock, FlexX, Fresno, Gold, Pmf, Score) to …

Bissantz, C.

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.

Nonapeptide Analogues Containing (R)-3-Hydroxybutanoate and β-Homoalanine Oligomers:  Synthesis and Binding Affinity to a Class I Major Histocompatibility Complex Protein

Crystal structures of antigenic peptides bound to class I MHC proteins suggest that chemical modifications of the central part of the bound peptide should not alter binding …

Poenaru, S.

Structure-Based Design of Nonnatural Ligands for the HLA-B27 Protein

X-ray studies as well as structure-activity relationships indicate that the central part of class I MHC-binding nonapeptides represents the main interaction site for a T cell …

Deadier, S.

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.

Synthesis of Oligo(3-hydroxybutanoate)(OHB)-Containing Peptides with High Binding Affinity to a Class-I-MHC Protein

In the center of the immune system, there are major histocompatibility (MHC) protein/nonapeptide complexes which are recognized by T cell.

Seebach, D.