Isothermal Calorimetry Study of the Interactions of Type I Antifreeze Proteins with a Lipid Model Membrane
In this paper, we report our study of thermodynamic parameters of the interactions of antifreeze proteins (AFP) type I and it short segments with DMPC unilamellar vesicles as model for cell membrane. The heat of interactions between AFP's and the model cell membrane were studied by Isothermal Titration Calorimetry (ITC) at temperatures above and below phase transition temperatures of the membrane. It is shown that heat of interactions is linearly dependent on the temperatures below the phase transition of the membrane and constant at temperatures above phase. The heat of interaction above phase transition is assigned to the interaction of the AFP with the membrane, while below phase transition the ordering effect of the AFP influence the heat of interaction.
No Supplementary Data
Document Type: Research Article
Publication date: 2010-06-01
More about this publication?
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.