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

Stefanie Barbirz, Marion Becker, Alexander Freiberg, Robert Seckler

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable β-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. A figure is presented.

Original languageEnglish (US)
Pages (from-to)169-173
Number of pages5
JournalMacromolecular Bioscience
Volume9
Issue number2
DOIs
StatePublished - Feb 11 2009

Fingerprint

Bacteriophage P22
Bacteriophages
Solenoids
Guanidine
Carbohydrates
Polysaccharides
Amino Acid Sequence
Maintenance
Proteins
Temperature
Denaturation
Amino acids
Amino Acids
Kinetics
saccharide-binding proteins

Keywords

  • Biofibers
  • Carbohydrate binding
  • Protein kinetic stability
  • Tailspike
  • Thermal properties

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Phage tailspike proteins with β-solenoid fold as thermostable carbohydrate binding materials. / Barbirz, Stefanie; Becker, Marion; Freiberg, Alexander; Seckler, Robert.

In: Macromolecular Bioscience, Vol. 9, No. 2, 11.02.2009, p. 169-173.

Research output: Contribution to journalArticle

Barbirz, Stefanie ; Becker, Marion ; Freiberg, Alexander ; Seckler, Robert. / Phage tailspike proteins with β-solenoid fold as thermostable carbohydrate binding materials. In: Macromolecular Bioscience. 2009 ; Vol. 9, No. 2. pp. 169-173.
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