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Birte Höcker

Group Leader

Birte.jpgHöcker Group (Protein Design)



MPI for Developmental Biology, Spemannstr. 35, 72076 Tübingen, Germany

Tel: +49 7071 601 322
Fax: +49 7071 601 305
E-Mail: Birte.Hoecker [AT] Tuebingen [DOT] MPG [DOT] de



Biography


  • PhD 2003 Biochemistry, Universität zu Köln, Germany
  • 2003-2005 Postdoctoral Fellow at Duke University Medical Center, USA
  • since 2006 Group leader at MPI for Developmental Biology, Germany


Publications


Schreier, B., Stumpp, C., Wiesner, S. & Höcker, B. (2009) Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci U S A, in press. [epub]

Malisi, C., Kohlbacher, O. & Höcker, B. (2009) Automated scaffold selection for enzyme design. Proteins 77, 74-83. [PubMed]

Claren, J., Malisi, C., Höcker, B. & Sterner, R. (2009) Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds. Proc Natl Acad Sci U S A 106, 3704-9. [PubMed]

Höcker, B., Lochner, A., Seitz, T., Claren, J. & Sterner, R. (2009) High-resolution crystal structure of an artificial (βα)8-barrel protein designed from identical half-barrels. Biochemistry 48, 1145-1147. [PubMed]

Höcker, B. Chapter 8: Structural frameworks suitable for engineering. In Protein Engineering Handbook. Eds. S.Lutz & U.T.Bornscheuer. Wiley-VCH 2008.

Bharat, T.A.M., Eisenbeis, S., Zeth, K. & Höcker, B. (2008) A βα-barrel built by the combination of fragments from different folds. Proc Natl Acad Sci U S A 105, 9942-7. [PubMed]

Höcker, B. (2008). Proteindesign und -engineering. Trendbericht in Biochemie und Molekularbiologie. Nachrichten aus der Chemie 56/3, 298-301. [GDCh]

Reetz, M.T., Rentzsch, M., Pletsch, A., Taglieber, A., Hollmann, F., Mondiere, R.J.G., Dickmann, N., Höcker, B., Cerrone, S., Haeger, M.C. & Sterner, R. (2008) A robust protein host for anchoring chelating ligands and organocatalysts. ChemBioChem 9, 552-64. [PubMed]

Tian, Y., Cuneo, M.J., Changela, A., Höcker, B., Beese, L.S. & Hellinga, H.W. (2007). Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein. Protein Sci 16, 2240-50. [PubMed]

Sterner, R. & Höcker, B. (2005). Catalytic versatility, stability, and evolution of the (βα)8-barrel enzyme fold. Chem Rev 105, 4038-55. [PubMed]

Höcker, B. (2005). Directed evolution of (βα)8-barrel enzymes. Biomol Eng 22, 31-8. [PubMed]

Höcker, B., Claren, J. & Sterner, R. (2004). Mimicking enzyme evolution by generating new (βα)8-barrels from (βα)4-half-barrels. Proc Natl Acad Sci U S A 101, 16448-53. [PubMed]

Raasch, C., Armbrecht, M., Streit, W., Höcker, B., Strater, N. & Liebl, W. (2002). Identification of residues important for NAD+ binding by the Thermotoga maritima α-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett 517, 267-71. [PubMed]

Höcker, B., Schmidt, S. & Sterner, R. (2002). A common evolutionary origin of two elementary enzyme folds. FEBS Lett 510, 133-5. [PubMed]

Höcker, B., Jürgens, C., Wilmanns, M. & Sterner, R. (2001). Stability, catalytic versatility and evolution of the (βα)8-barrel fold. Curr Opin Biotechnol 12, 376-81. [PubMed]

Höcker, B., Beismann-Driemeyer, S., Hettwer, S., Lustig, A. & Sterner, R. (2001). Dissection of a (βα)8-barrel enzyme into two folded halves. Nat Struct Biol 8, 32-6. [PubMed]

Henn-Sax, M., Höcker, B., Wilmanns, M. & Sterner, R. (2001). Divergent evolution of (βα)8-barrel enzymes. Biol Chem 382, 1315-20. [PubMed]

 


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last modified 2009-10-16