A variety of computational strategies have been developed to face the challenges in determining the native conformations of proteins by exploring (scanning) the potential energy of the conformational space (c-space). According to the funnel hypothesis of the protein potential energy landscape, the native-protein conformation (3D structure) is at the bottom of the funnel at the lowest free energy, i.e., a global energy minimum. However, it has progressed through the years into an operable challenge with amenable and reasonably accurate predictions in many cases. Protein 3D-structure folding from a simple sequence of amino acids was seen as a very difficult problem in the past. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. 18-10251S) and CEITEC 2020 (LQ1601) for financial support of this work. 759585), the Czech Science Agency (project no. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: We gratefully acknowledge the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement no. PLoS Comput Biol 16(4):Įditor: Francis Ouellette, University of Toronto, CANADAĬopyright: © 2020 Haddad et al. Citation: Haddad Y, Adam V, Heger Z (2020) Ten quick tips for homology modeling of high-resolution protein 3D structures.
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