We consider d = 2 Ising strip with surface fields acting on boundary spins. Using the properties of the transfer matrix spectrum we identify two pseudotransition temperatures and show that they satisfy similar scaling relations as expected for real transition temperatures in strips with d > 2. The solvation force between the boundaries of the strip is analysed as a function of temperature, surface fields and the width of the strip. For large widths the solvation force can be described by scaling functions in three different regimes: in the vicinity of the critical wetting temperature of 2D semi-infinite system, in the vicinity of the bulk critical temperature, and in the regime of weak surface fields where the critical wetting temperature tends towards the bulk critical temperature. The properties of the relevant scaling functions are discussed.

The solvation force for two-dimensional Ising strips is calculated via exact diagonalization of the transfer matrix in two cases: the symmetric case corresponds to identical surface fields and the antisymmetric case to exactly opposite surface fields. In the symmetric case the solvation force is always negative (attractive), while in the antisymmetric case the solvation force is positive (repulsive) at high temperatures and negative at low temperatures. It changes sign close to the critical wetting temperature characterizing the semi-infinite system. The properties of the solvation force are discussed, and the scaling function describing its dependence on temperature, surface field, and strip's width is proposed.

The natural environment of proteins is the polar aquatic environment and the hydrophobic (amphipathic) environment of the membrane. The fuzzy oil drop model (FOD) used to characterize water-soluble proteins, as well as its modified version FOD-M, enables a mathematical description of the presence and influence of diverse environments on protein structure. The present work characterized the structures of membrane proteins, including those that act as channels, and a water-soluble protein for contrast. The purpose of the analysis was to verify the possibility that an external force field can be used in the simulation of the protein-folding process, taking into account the diverse nature of the environment that guarantees a structure showing biological activity.

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We consider two-dimensional Ising strip bounded by two planar, inhomogeneous walls. The inhomogeneity of each wall is modeled by a magnetic field acting on surface spins. It is equal to +h1 except for a group of N1 sites where it is equal to −h1. The inhomogeneities of the upper and lower wall are shifted with respect to each other by a lateral distance L. Using exact diagonalization of the transfer matrix, we study both the lateral and normal critical Casimir forces as well as magnetization profiles for a wide range of temperatures and system parameters. The lateral critical Casimir force tends to reduce the shift between the inhomogeneities, and the excess normal force is attractive. Upon increasing the shift L we observe, depending on the temperature, three different scenarios of breaking of the capillary bridge of negative magnetization connecting the inhomogeneities of the walls across the strip. As long as there exists a capillary bridge in the system, the magnitude of the excess total critical Casimir force is almost constant, with its direction depending on L. By investigating the bridge morphologies we have found a relation between the point at which the bridge breaks and the inflection point of the force. We provide a simple argument that some of the properties reported here should also hold for a whole range of different models of the strip with the same type of inhomogeneity.