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Birte Höcker

Position: Project Leader
Unit: Höcker
Phone: +49 7071 601 322
Picture of Höcker, Birte

Professional positions

2006-presentLeader of an independent research group, MPI for Developmental Biology
2003-2005Postdoctoral work at Duke University Medical Center, USA

2003PhD in Biochemistry, Universität zu Köln, Germany
1999Diplom in Biology, Universität Göttingen, Germany

Awards & Funding

2007-2010DFG research grant "Evolutionary relationship of two elementary protein folds"
2010-2013DFG research grant "Computational tools for the design of ligand binding in proteins"
2010Biology prize of the Akademie der Wissenschaften zu Göttingen
2011-2014 DFG research grant "Evolutionary relationship of two elementary protein folds" (renewal)
2011-Part of the International Max Planck Research School (IMPRS) "From Molecules to Organisms"
2013-Member of the Zentrum für Bioinformatik (ZBIT) Tübingen
2014-2016DFG research grant "Computational tools for the design of ligand binding in proteins" (renewal)
2015-2020ERC Consolidator Grant "Protein design from subdomain sized fragments"
2015Otto-Meyerhof Award of the GBM


Stiel, A., Feldmeier, K. & Höcker, B. (2014) Identification of protein scaffolds for enzyme design using ScaffoldSelection. Methods Mol Biol 1216:183-96. [PubMed]
Farias-Rico, J.A., Schmidt, S. & Höcker, B. (2014) Evolutionary relationship of two ancient protein superfolds. Nature Chem Biol 10:710-5. [PubMed, f1000MPGnews]

Höcker, B. (2014) Design of proteins from smaller fragments - learning from evolution. Curr Opin Struc Biol 27:56-62.  [PubMed]

Scheib, U., Shanmugaratnam, S., Farias-Rico, J.A. & Höcker, B. (2014) Change in protein-ligand specificity through binding pocket grafting. J Struc Biol 185: 186-92. doi: 10.1016/j.jsb.2013.06.002. Epub 2013 Jun17. [PubMed]

Höcker, B. & Midelfort, K. (2014) Designing protein function - Macromolecular design. J Struc Biol 185:135. [PubMed]

Editorial to the special issue on "Macromolecular Design"- edited by Katarina Midelfort & myself


Feldmeier, K. & Höcker, B. (2013) Computational protein design of ligand binding and catalysis. Curr Opin Chem Biol 17:929–933. [PubMed]
Farias-Rico, J.A. & Höcker, B. (2013) Design of chimeric proteins by combination of subdomain-sized fragments. Methods Enzymol 523, 389-405. [PubMed]
Meier, M.M.,Rajendran, C., Malisi, C., Fox, N.G., Xu, C., Schlee, S., Barondeau, D.P., Höcker, B., Sterner, R. & Raushel, F.M. (2013) Molecular Engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template. J Am Chem Soc 135: 11670-7. [PubMed]
Höcker, B. (2013) Engineering chimaeric proteins from fold fragments: 'hopeful monsters' in protein design. Biochem Soc Trans 41: 1137-40. [PubMed]
Webcast of the presentation entitled 'Engineering proteins from fold fragments' presented at the joint Biochemical Society / Protein Society Focused Meeting 'Protein engineering: new approaches and applications', held in April 2013. [BiochemSociety]


Malisi, C., Schumann, M., Toussaint, N.C., Kageyama, J., Kohlbacher, O. & Höcker, B. (2012) Binding pocket optimization by computational protein design. PLoS One, 7(12):e52505. [PubMed].

Höcker, B. (2012) A toolbox for protein design. Nature 491: 204-5. [PubMed] - News & Views on Koga et al. (2012): Principles for designing ideal protein structures.
Shanmugaratnam, S., Eisenbeis, S. & Höcker, B. (2012) A highly stable protein chimera built from fragments of different folds. Protein Eng Des Sel 25: 699-703. [PubMed]
Höcker, B. (2012) A metalloenzyme reloaded. Nature Chem Biol 8: 224-5. [PubMed] - News & Views on Khare et al. (2012): Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis.
Eisenbeis, S., Proffitt, W., Coles, M., Truffault, V., Shanmugaratnam, S., Meiler, J. & Höcker, B. (2012) The potential of fragment recombination for the rational design of proteins. J Am Chem Soc 134: 4019-22. [PubMed]   f1000


Höcker, B. Einblicke in die Mechanismen der Evolution durch Protein Design. Jahrbuch der Akademie der Wissenschaften zu Göttingen 2011, S. 183-187, De Gruyter.
Malisi, C., Stiel, A.C. & Höcker, B. (2011) Enzyme am Reißbrett. BIOspektrum 7: 736-8. [BIOspektrum]


Schreier, B. & Höcker, B. (2010) Engineering the enolase magnesium II binding site: implications for its evolution. Biochemistry 49: 7582-9. [PubMed]
Eisenbeis, S. & Höcker, B. (2010) Evolutionary mechanism as a template for protein engineering. J Pep Sci 16: 538-44. [PubMed]
Höcker, B. (2010) Metals make proteins stick. Chem Biol 17: 103-4. [PubMed] - Preview on Salgado et al. (2010): Metal templated design of protein interfaces.
Höcker, B. Mechanismen der Evolution als Matrize für Protein Engineering (Forschungsbericht 2010 - MPI für Entwicklungsbiologie) [MPG website]


Schreier, B., Stumpp, C., Wiesner, S. & Höcker, B. (2009) Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci USA 106: 18491-6. [PubMed]     -Media coverage on this paper: "Protein design papers challenged" in Nature News & "Designed proteins debunked?" in The Scientist   f1000
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 (ßa)8-barrel protein scaffolds. Proc Natl Acad Sci USA 106: 3704-9. [PubMed]   f1000
Höcker, B., Lochner, A., Seitz, T., Claren, J. & Sterner, R. (2009) High-resolution crystal structure of an artificial (ßa)8-barrel protein designed from identical half-barrels. Biochemistry 48: 1145-1147. [PubMed]


Bharat, T.A.M., Eisenbeis, S., Zeth, K. & Höcker, B. (2008) A ßa-barrel built by the combination of fragments from different folds. Proc Natl Acad Sci USA 105: 9942-7. [PubMed]   f1000
Höcker, B. (2008). Proteindesign und -engineering. Trendbericht in Biochemie und Molekularbiologie. Nachrichten aus der Chemie 56/3: 298-301. [GDCh]
Höcker, B. Chapter 8: Structural frameworks suitable for engineering. In Protein Engineering Handbook. Eds. S.Lutz & U.T.Bornscheuer. Wiley-VCH 2008.
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]

2005 - 2007

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 (ßa)8-barrel enzyme fold. Chem Rev 105: 4038-55. [PubMed]
Höcker, B. (2005). Directed evolution of (ßa)8-barrel enzymes. Biomol Eng 22: 31-8. [PubMed]

2001 - 2004

Höcker, B., Claren, J. & Sterner, R. (2004). Mimicking enzyme evolution by generating new (ßa)8-barrels from (ßa)4-half-barrels. Proc Natl Acad Sci USA 101: 16448-53. [PubMed]     f1000
Raasch, C., Armbrecht, M., Streit, W., Höcker, B., Strater, N. & Liebl, W. (2002). Identification of residues important for NAD+ binding by the Thermotoga maritima a-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., Beismann-Driemeyer, S., Hettwer, S., Lustig, A. & Sterner, R. (2001). Dissection of a (ßa)8-barrel enzyme into two folded halves. Nature Struct Biology 8: 32-6. [PubMed]
Höcker, B., Jürgens, C., Wilmanns, M. & Sterner, R. (2001). Stability, catalytic versatility and evolution of the (ßa)8-barrel fold. Curr Opin Biotechnol 12: 376-81. [PubMed]
Henn-Sax, M., Höcker, B., Wilmanns, M. & Sterner, R. (2001). Divergent evolution of (ßa)8-barrel enzymes. Biol Chem 382: 1315-20. [PubMed]

before 2000

Whiteway, J., Koziarz, P., Veall, J., Sanhu, N., Kumar, P., Höcker, B. & Lambert, I.B. (1998). Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. J Bacteriol 180: 5529-39. [PubMed]