no code implementations • 16 Apr 2024 • Benjamin J. Livesey, Mihaly Badonyi, Mafalda Dias, Jonathan Frazer, Sushant Kumar, Kresten Lindorff-Larsen, David M. McCandlish, Rose Orenbuch, Courtney A. Shearer, Lara Muffley, Julia Foreman, Andrew M. Glazer, Ben Lehner, Debora S. Marks, Frederick P. Roth, Alan F. Rubin, Lea M. Starita, Joseph A. Marsh
Computational methods for assessing the likely impacts of mutations, known as variant effect predictors (VEPs), are widely used in the assessment and interpretation of human genetic variation, as well as in other applications like protein engineering.
no code implementations • 2 Mar 2023 • Chapin E. Cavender, David A. Case, Julian C. -H. Chen, Lillian T. Chong, Daniel A. Keedy, Kresten Lindorff-Larsen, David L. Mobley, O. H. Samuli Ollila, Chris Oostenbrink, Paul Robustelli, Vincent A. Voelz, Michael E. Wall, David C. Wych, Michael K. Gilson
This review article provides an overview of structurally oriented, experimental datasets that can be used to benchmark protein force fields, focusing on data generated by nuclear magnetic resonance (NMR) spectroscopy and room temperature (RT) protein crystallography.
no code implementations • 10 Dec 2021 • F. Emil Thomasen, Kresten Lindorff-Larsen
Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a high level of structural heterogeneity and are best described by ensembles consisting of multiple conformations with associated thermodynamic weights.
no code implementations • 1 Jun 2021 • Kresten Lindorff-Larsen, Birthe B. Kragelund
Intrinsically disordered proteins (IDPs) constitute a broad set of proteins with few uniting and many diverging properties.