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Phage tailspike proteins with beta-solenoid fold as thermostable carbohydrate binding materials

  • We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable beta-solenoid folds and similarly high kinetic stability in spite of different amino acid sequences. As tailspikes bind polysaccharides to recognize the bacterial host cell, their stability is required for maintenance of bacteriophage infectivity under harsh extracellular conditions. They resist denaturation by SDS at ambient temperature and their unfolding is slow even in 6 m guanidinium hydrochloride (GdmHCl). This makes them interesting candidates for very stable carbohydrate binding protein materials.

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Author details:Stefanie BarbirzORCiDGND, Marion Becker, Alexander Freiberg, Robert SecklerORCiDGND
URL:http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%291616-5195
DOI:https://doi.org/10.1002/mabi.200800278
ISSN:1616-5187
Publication type:Article
Language:English
Year of first publication:2009
Publication year:2009
Release date:2017/03/25
Source:Macromolecular bioscience. - ISSN 1616-5187. - 9 (2009), 2, S. 169 - 173
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer review:Referiert
Publishing method:Open Access
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