Ontology highlight
ABSTRACT:
SUBMITTER: Ebbinghaus S
PROVIDER: S-EPMC3400764 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Ebbinghaus Simon S Meister Konrad K Prigozhin Maxim B MB Devries Arthur L AL Havenith Martina M Dzubiella Joachim J Gruebele Martin M
Biophysical journal 20120717 2
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 pe ...[more]