ArticleStructure (London, England : 1993)2015
Parsimony in Protein Conformational Change.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Synergism between x-ray crystallography and NMR residual dipolar couplings in characterizing protein dynamics.Structural dynamics (Melville, N.Y.) · 2023Article
- hdANM: a new comprehensive dynamics model for protein hinges.Biophysical journal · 2021Article
- FragFit: a web-application for interactive modeling of protein segments into cryo-EM density maps.Nucleic acids research · 2018Article
- A fragment based method for modeling of protein segments into cryo-EM density maps.BMC bioinformatics · 2017Article
- The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide.Molecular therapy. Methods & clinical development · 2017Article
- The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.Structure (London, England : 1993) · 2016Article
Corrections and comments
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Authors and funding
5 authors.
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Abstract
Protein conformational change is analyzed by finding the minimalist backbone torsion angle rotations that superpose crystal structures within experimental error. Of several approaches for enforcing parsimony during flexible least-squares superposition, an ℓ(1)-norm restraint provided greatest consistency with independent indications of flexibility from nuclear magnetic resonance relaxation dispersion and chemical shift perturbation in arginine kinase and four previously studied systems. Crystallographic cross-validation shows that the dihedral parameterization describes conformational change more accurately than rigid-group approaches. The rotations that superpose the principal elements of structure constitute a small fraction of the raw (φ, ψ) differences that also reflect local conformation and experimental error. Substantial long-range displacements can be mediated by modest dihedral rotations, accommodated even within α helices and β sheets without disruption of hydrogen bonding at the hinges. Consistency between ligand-associated and intrinsic motions (in the unliganded state) implies that induced changes tend to follow low-barrier paths between conformational sub-states that are in intrinsic dynamic equilibrium.
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Registered trials
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