title: Functional importance of short-range binding and long-range solvent interactions in helical antifreeze peptides.
abstract: Short-range ice binding and long-range solvent perturbation both have been implicated in the activity of antifreeze proteins and antifreeze glycoproteins. We study these two mechanisms for activity of winter flounder antifreeze peptide. Four mutants are characterized by freezing point hysteresis (activity), circular dichroism (secondary structure), Förster resonance energy transfer (end-to-end rigidity), molecular dynamics simulation (structure), and terahertz spectroscopy (long-range solvent perturbation). Our results show that the short-range model is sufficient to explain the activity of our mutants, but the long-range model provides a necessary condition for activity: the most active peptides in our data set all have an extended dynamical hydration shell. It appears that antifreeze proteins and antifreeze glycoproteins have reached different evolutionary solutions to the antifreeze problem, utilizing either a few precisely positioned OH groups or a large quantity of OH groups for ice binding, assisted by long-range solvent perturbation.
authors.affiliation: Department of Physical Chemistry II, Ruhr-Universität Bochum, Bochum, Germany.
authors.forename: Simon
authors.initials: S
authors.lastname: Ebbinghaus
authors.forename: Konrad
authors.initials: K
authors.lastname: Meister
authors.forename: Maxim B
authors.initials: MB
authors.lastname: Prigozhin
authors.forename: Arthur L
authors.initials: AL
authors.lastname: Devries
authors.forename: Martina
authors.initials: M
authors.lastname: Havenith
authors.forename: Joachim
authors.initials: J
authors.lastname: Dzubiella
authors.forename: Martin
authors.initials: M
authors.lastname: Gruebele
mesh_terms: D000042:Absorption; D000595:Amino Acid Sequence; D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry* / Q000378:metabolism*; D002021:Buffers; D002942:Circular Dichroism; D005432:Flounder; D031541:Fluorescence Resonance Energy Transfer; D005615:Freezing; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012997:Solvents / Q000378:metabolism*; D014867:Water / Q000737:chemistry
chemical_list: D021301:Antifreeze Proteins; D002021:Buffers; D012997:Solvents; D014867:Water