Journal
MACROMOLECULAR BIOSCIENCE
Volume 9, Issue 2, Pages 169-173Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/mabi.200800278
Keywords
biofibers; carbohydrate binding; protein kinetic stability; tailspike; thermal properties
Funding
- Deutsche Forschungsgemeinschaft [Se 517/16]
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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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