Coiled-Coils in Phage Display Screening: Insight into Exceptional Selectivity Provided by Molecular Dynamics
- Jérémie Mortier
- ,
- Elisabeth K. Nyakatura
- ,
- Oliver Reimann
- ,
- Susanne Huhmann
- ,
- Jan O. Daldrop
- ,
- Carsten Baldauf
- ,
- Gerhard Wolber
- ,
- Markus S. Miettinen
- , and
- Beate Koksch
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† Department of Biology, Chemistry and Pharmacy, Freie Universität Berlin, Takustraße 3, 14195 Berlin, Germany
‡ Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany
|| Fritz Haber Institute der MPG, Faradayweg 4-6, 14195 Berlin, Germany
*E-mail: [email protected]. Fax: +49 30 83855644. Tel.: +49-030-83855344 (B.K.).
*E-mail: [email protected]. Tel.: +49 30 83858090 (J.M.).
Abstract
Involved in numerous key biological functions, protein helix–helix interactions follow a well-defined intermolecular recognition pattern. The characteristic structure of the α-helical coiled-coil allows for the specific randomization of clearly defined interaction partners within heteromeric systems. In this work, a rationally designed heterodimeric coiled-coil was used to investigate potential factors influencing the sequence selectivity in interhelical interactions.
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