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Jeschke G. Characterization of Protein Conformational Changes with Sparse Spin-Label Distance Constraints. J Chem Theory Comput. 2012;8(10):3854-63doi: 10.1021/ct300113z.
Jeschke, G. (2012). Characterization of Protein Conformational Changes with Sparse Spin-Label Distance Constraints. Journal of chemical theory and computation, 8(10), 3854-63. https://doi.org/10.1021/ct300113z
Jeschke, G. "Characterization of Protein Conformational Changes with Sparse Spin-Label Distance Constraints." Journal of chemical theory and computation vol. 8,10 (2012): 3854-63. doi: https://doi.org/10.1021/ct300113z
Jeschke G. Characterization of Protein Conformational Changes with Sparse Spin-Label Distance Constraints. J Chem Theory Comput. 2012 Oct 09;8(10):3854-63. doi: 10.1021/ct300113z. Epub 2012 May 03. PMID: 26593026.
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J Chem Theory Comput. 2012 Oct 09;8(10):3854-63. doi: 10.1021/ct300113z. Epub 2012 May 03.

Characterization of Protein Conformational Changes with Sparse Spin-Label Distance Constraints.

Journal of chemical theory and computation

G Jeschke

Affiliations

  1. Lab. Phys. Chem., ETH Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland.

PMID: 26593026 DOI: 10.1021/ct300113z

Abstract

The combination of site-directed spin labeling with pulse EPR distance measurements can provide a moderate number of distance constraints on the nanometer length scale for proteins in different states. By adapting an existing algorithm (Zheng, W.; Brooks, B. R. Biophys. J. 2006, 90, 4327) to the problem, we address the question to what extent conformational change can be characterized when the protein structure is known for one of the states, whereas only a sparse set of distance constraints between spin labels is available for the other state. We find that the type and general direction of the conformational change can be recognized, while the amplitude may be uncertain.

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