Molecular Sequence Data

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.

• Dec 1, 2001 • 1 min read

Solution structure of a conformationally constrained Arg-Gly-Asp-like motif inserted into the alpha/beta scaffold of leiurotoxin I.

A monoclonal antibody, AC7, directed against the RGD-binding site of the GPIIIa subunit of the platelet fibrinogen receptor, interacts with activated platelet.

Kellenberger, E.

• Mar 1, 1999 • 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

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

Solution structure of a conformationally constrained Arg-Gly-Asp-like motif inserted into the alpha/beta scaffold of leiurotoxin I.

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.