One bead per residue can describe all-atom protein structures
Authors:
- 23 November 2023
- Vol. 32 (1) , 97-111.e6
Abstract
No abstract availableKeywords
Funding Information
- National Science Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (R35 GM126948)
This publication has 85 references indexed in Scilit:
- Improving the Physical Realism and Structural Accuracy of Protein Models by a Two-Step Atomic-Level Energy MinimizationBiophysical Journal, 2011
- PRIMO/PRIMONA: A coarse‐grained model for proteins and nucleic acids that preserves near‐atomistic accuracyProteins: Structure, Function, and Bioinformatics, 2009
- Conformation Dependence of Backbone Geometry in ProteinsStructure, 2009
- Improved prediction of protein side‐chain conformations with SCWRL4Proteins: Structure, Function, and Bioinformatics, 2009
- REMO: A new protocol to refine full atomic protein models from C‐alpha traces by optimizing hydrogen‐bonding networksProteins: Structure, Function, and Bioinformatics, 2009
- Fast procedure for reconstruction of full‐atom protein models from reduced representationsJournal of Computational Chemistry, 2008
- Discovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked ChainsJournal of Molecular Biology, 2007
- EMAN2: An extensible image processing suite for electron microscopyJournal of Structural Biology, 2007
- UCSF Chimera—A visualization system for exploratory research and analysisJournal of Computational Chemistry, 2004
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983