title: Structure of solvation water around the active and inactive regions of a type III antifreeze protein and its mutants of lowered activity.
abstract: Water molecules from the solvation shell of the ice-binding surface are considered important for the antifreeze proteins to perform their function properly. Herein, we discuss the problem whether the extent of changes of the mean properties of solvation water can be connected with the antifreeze activity of the protein. To this aim, the structure of solvation water of a type III antifreeze protein from Macrozoarces americanus (eel pout) is investigated. A wild type of the protein is used, along with its three mutants, with antifreeze activities equal to 54% or 10% of the activity of the native form. The solvation water of the ice-binding surface and the rest of the protein are analyzed separately. To characterize the structure of solvation shell, parameters describing radial and angular characteristics of the mutual arrangement of the molecules were employed. They take into account short-distance (first hydration shell) or long-distance (two solvation shells) effects. The obtained results and the comparison with the results obtained previously for a hyperactive antifreeze protein from Choristoneura fumiferana lead to the conclusion that the structure and amino acid composition of the active region of the protein evolved to achieve two goals. The first one is the modification of the properties of the solvation water. The second one is the geometrical adjustment of the protein surface to the specific crystallographic plane of ice. Both of these goals have to be achieved simultaneously in order for the protein to perform its function properly. However, they seem to be independent from one another in a sense that very small antifreeze activity does not imply that properties of water become different from the ones observed for the wild type. The proteins with significantly lower activity still modify the mean properties of solvation water in a right direction, in spite of the fact that the accuracy of the geometrical match with the ice lattice is lost because of the mutations. Therefore, we do not observe any correlation between the antifreeze activity and the extent of modification of the properties of solvation water.
authors.affiliation: Faculty of Chemistry, Department of Physical Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
authors.forename: Joanna
authors.initials: J
authors.lastname: Grabowska
authors.affiliation: Faculty of Chemistry, Department of Physical Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
authors.forename: Anna
authors.initials: A
authors.lastname: Kuffel
authors.affiliation: Faculty of Chemistry, Department of Physical Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
authors.forename: Jan
authors.initials: J
authors.lastname: Zielkiewicz
mesh_terms: D000818:Animals; D021343:Antifreeze Proteins, Type III / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D057506:Arthropod Antennae / Q000737:chemistry; D020134:Catalytic Domain; D009154:Mutation; D010473:Perciformes; D012997:Solvents / Q000737:chemistry; D014867:Water / Q000737:chemistry*
chemical_list: D021343:Antifreeze Proteins, Type III; D012997:Solvents; D014867:Water