Informationssystem der Friedrich-Alexander-Universität Erlangen-Nürnberg © Config eG 
Lehrstuhl für Biotechnik (Proteinstruktur und -design)
Anschrift: MVC, Henkestrasse 91, 91052 Erlangen
Tel.:+49 9131 85-23081Fax:+49 9131 85-23080

Research interests
De novo structure determination
Classical crystallography is used to determine the crystal structures of human plasma proteins such as transport proteins, growth factors and cell surface receptors. Recent work includes crystal structures of vascular endothelial growth factor (VEGF) and sex hormone-binding globulin (SHBG). Present work aims to unravel how domains similar to those of SHBG mediate protein protein interactions during cell signaling.
Probing protein architecture/protein design
Cystine knots are present in a number of different proteins such as growth factors, small inhibitor proteins and the antimicrobial cyclotides. The knot motif consists of three intertwined disulfide bridges and we have recently challenged the general assumption that this motif is important for protein stability. Our current aim is to develop novel computational tools for the general use in protein design. The tools will be validated trying to repack and retie the knot of the cystine knot growth factors.

Prof. Dr. Yves Muller

Dipl.-Chem. Claudia Egerer-Sieber

Wiss. Mitarbeiter
Mark Kriegel, M. Sc.
Dr. rer. nat. Martin Stiebritz

  • keine Forschungsprojekte eingetragen
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