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Townsend PD, Rodgers TL, Pohl E, et al. Global low-frequency motions in protein allostery: CAP as a model system. Biophys Rev. 2015;7(2):175-182doi: 10.1007/s12551-015-0163-9.
Townsend, P. D., Rodgers, T. L., Pohl, E., Wilson, M. R., McLeish, T. C., & Cann, M. J. (2015). Global low-frequency motions in protein allostery: CAP as a model system. Biophysical reviews, 7(2), 175-182. https://doi.org/10.1007/s12551-015-0163-9
Townsend, Philip D, et al. "Global low-frequency motions in protein allostery: CAP as a model system." Biophysical reviews vol. 7,2 (2015): 175-182. doi: https://doi.org/10.1007/s12551-015-0163-9
Townsend PD, Rodgers TL, Pohl E, Wilson MR, McLeish TC, Cann MJ. Global low-frequency motions in protein allostery: CAP as a model system. Biophys Rev. 2015;7(2):175-182. doi: 10.1007/s12551-015-0163-9. Epub 2015 Feb 04. PMID: 26000062; PMCID: PMC4432019.
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Biophys Rev. 2015;7(2):175-182. doi: 10.1007/s12551-015-0163-9. Epub 2015 Feb 04.

Global low-frequency motions in protein allostery: CAP as a model system.

Biophysical reviews

Philip D Townsend, Thomas L Rodgers, Ehmke Pohl, Mark R Wilson, Tom C B McLeish, Martin J Cann

Affiliations

  1. Biophysical Sciences Institute, Durham University, Durham, UK ; School of Biological and Biomedical Sciences, Durham University, Durham, UK.
  2. Biophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK ; School of Chemical Engineering and Analytical Sciences, University of Manchester, Manchester, UK.
  3. Biophysical Sciences Institute, Durham University, Durham, UK ; School of Biological and Biomedical Sciences, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK.
  4. Biophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK.
  5. Biophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK ; Department of Physics, Durham University, Durham, UK.

PMID: 26000062 PMCID: PMC4432019 DOI: 10.1007/s12551-015-0163-9

Abstract

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of

Keywords: Allostery; Catabolite activator protein; Dynamics; Elastic network model; Normal modes; Protein

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