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Rapid Simulation of Unprocessed DEER Decay Data for Protein Fold Prediction.
Del Alamo, Diego; Tessmer, Maxx H; Stein, Richard A; Feix, Jimmy B; Mchaourab, Hassane S; Meiler, Jens.
Affiliation
  • Del Alamo D; Department of Chemistry and Center for Structural Biology; Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee.
  • Tessmer MH; Department of Microbiology and Immunology.
  • Stein RA; Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee.
  • Feix JB; Department of Biophysics, Medical College of Wisconsin, Milwaukee, Wisconsin.
  • Mchaourab HS; Department of Chemistry and Center for Structural Biology; Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee.
  • Meiler J; Department of Chemistry and Center for Structural Biology; Institut for Drug Discovery, Leipzig University, Leipzig, Germany. Electronic address: jens.meiler@vanderbilt.edu.
Biophys J ; 118(2): 366-375, 2020 01 21.
Article in En | MEDLINE | ID: mdl-31892409
Despite advances in sampling and scoring strategies, Monte Carlo modeling methods still struggle to accurately predict de novo the structures of large proteins, membrane proteins, or proteins of complex topologies. Previous approaches have addressed these shortcomings by leveraging sparse distance data gathered using site-directed spin labeling and electron paramagnetic resonance spectroscopy to improve protein structure prediction and refinement outcomes. However, existing computational implementations entail compromises between coarse-grained models of the spin label that lower the resolution and explicit models that lead to resource-intense simulations. These methods are further limited by their reliance on distance distributions, which are calculated from a primary refocused echo decay signal and contain uncertainties that may require manual refinement. Here, we addressed these challenges by developing RosettaDEER, a scoring method within the Rosetta software suite capable of simulating double electron-electron resonance spectroscopy decay traces and distance distributions between spin labels fast enough to fold proteins de novo. We demonstrate that the accuracy of resulting distance distributions match or exceed those generated by more computationally intensive methods. Moreover, decay traces generated from these distributions recapitulate intermolecular background coupling parameters even when the time window of data collection is truncated. As a result, RosettaDEER can discriminate between poorly folded and native-like models by using decay traces that cannot be accurately converted into distance distributions using regularized fitting approaches. Finally, using two challenging test cases, we demonstrate that RosettaDEER leverages these experimental data for protein fold prediction more effectively than previous methods. These benchmarking results confirm that RosettaDEER can effectively leverage sparse experimental data for a wide array of modeling applications built into the Rosetta software suite.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Monte Carlo Method / Protein Folding / Electron Spin Resonance Spectroscopy Type of study: Health_economic_evaluation / Prognostic_studies / Risk_factors_studies Language: En Journal: Biophys J Year: 2020 Type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Monte Carlo Method / Protein Folding / Electron Spin Resonance Spectroscopy Type of study: Health_economic_evaluation / Prognostic_studies / Risk_factors_studies Language: En Journal: Biophys J Year: 2020 Type: Article