| Folding and aggregation of proteins, the interaction between proteins and membranes, as well as the adsorption of organic soft matter to inorganic solid substrates belong to the most interesting challenges in understanding structure and function of complex macromolecules. This is reasoned by the interdisciplinary character of the associated questions ranging from the molecular origin of the loss of biological functionality as, for example, in Alzheimer's disease, to the development of organic circuits for biosensory applications. In this talk, results of computer simulations of mesoscopic models for proteins, protein aggregates, and hybrid systems of soft and solid condensed matter are presented. The simplicity of the coarse-grained models allows for a more universal description of the notoriously difficult problem of protein folding. In this approach, classifications of structure formation processes with respect to the conformational pseudophases are possible. This is similar in aggregation and adsorption processes, where the individual folding propensity is influenced by external forces. The main problem in studies of conformational transitions is that the sequences of amino acids, proteins are built up of, are necessarily of finite length and, therefore, a thermodynamic limit does not exist. Thus, structural transitions are not phase transitions in the strict thermodynamic sense and the analysis of "universal" aspects is intricate. Nonetheless, apparent small-system effects are not only fascinating because of their relevance in nature. These effects are also interesting from the more basic approach of understanding thermodynamics of conformational transitions from perspectives of different statistical ensembles. One such example to be presented is the phase-separation process of aggregation of a few small proteins which exhibits unconventional features that favor multicanonical and microcanonical analyses compared to the standard canonical approach. |
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