Assessing the quality of modelled 3D protein structures using the ModFOLD serverRoche, D. B., Buenavista, M. T. and McGuffin, L. J. ORCID: https://orcid.org/0000-0003-4501-4767 (2014) Assessing the quality of modelled 3D protein structures using the ModFOLD server. In: Protein Structure Prediction. Methods in Molecular Biology, 1137. Springer, pp. 83-103. ISBN 9781493903658 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1007/978-1-4939-0366-5_7 Abstract/SummaryModel quality assessment programs (MQAPs) aim to assess the quality of modelled 3D protein structures. The provision of quality scores, describing both global and local (per-residue) accuracy are extremely important, as without quality scores we are unable to determine the usefulness of a 3D model for further computational and experimental wet lab studies.Here, we briefly discuss protein tertiary structure prediction, along with the biennial Critical Assessment of Techniques for Protein Structure Prediction (CASP) competition and their key role in driving the field of protein model quality assessment methods (MQAPs). We also briefly discuss the top MQAPs from the previous CASP competitions. Additionally, we describe our downloadable and webserver-based model quality assessment methods: ModFOLD3, ModFOLDclust, ModFOLDclustQ, ModFOLDclust2, and IntFOLD-QA. We provide a practical step-by-step guide on using our downloadable and webserver-based tools and include examples of their application for improving tertiary structure prediction, ligand binding site residue prediction, and oligomer predictions.
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