Homology modeling of protein structures Homology modeling is a protein structure modeling method that relies on the principle of structural similarity between homologous proteins. Once a homolog with an experimentally-resolved structure of a protein sequence is available, it is in principle to generate a structure model using homology modeling. There are a variety of homology modeling tools, freely available for research purposes, such as SWISSMODEL and Modeller. In this exercise, we explore SWISS-MODEL web interface. Major Facilitatory Superfamily (MFS) proteins are secondary active efflux pumps found in cell membranes of many organisms. These proteins perform the critical function of maintaining homeostasis of a biological cell, and are also involved in resistance against drugs in cancer cells or against antibiotics (if MFS protein is found in a bacterial species). 1) Make a quick literature search on the conformational (transport) cycle of MFS transporters*, and describe your findings briefly (e.g. up to five sentences). 2) Search the literature on MFS transporters, and identify at least one MFS.protein with no experimentally resolved structure. You can find a list of MFS transporters here: 3) Provide a very brief description of function of this protein based oij its UniProt entry. 4) Generate at least three different homology models of this protein using the SWISS-MODEL web interface (swissmodel.expasy.org) (Hint: you may want to focus on selection of templates detected by SWISS-MODEL, so do not directly "Build Model", "Search for Templates" instead. By doing this, you can use different templates each time, resulting in different homology models. 5) Assess the quality of the generated models using the "Structure Assessment" feature of SWISSMODEL. Did the resulting structure cover the whole sequence of the template structure? What is the sequence identity between your target sequence and the template sequence? Which of the resulting models were physically more plausible? Make sure you report the Ramachandran plots and include the results of the Ramachandran plot in your discussion. "Hint for your discussion: The energy landscape of MFS proteins include multiple energy minima, i. e. the protein switches back and forth between "semi-stable" conformational states