caa a22 4500 60624297X CHVBK 20210128101321.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s12551-015-0163-9 doi (NATIONALLICENCE)springer-10.1007/s12551-015-0163-9 Global low-frequency motions in protein allostery: CAP as a model system [Elektronische Daten] [Philip Townsend, Thomas Rodgers, Ehmke Pohl, Mark Wilson, Tom McLeish, Martin Cann] 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 Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding. The Author(s), 2015 Protein nationallicence Allostery nationallicence Dynamics nationallicence Catabolite activator protein nationallicence Normal modes nationallicence Elastic network model nationallicence Townsend Philip Biophysical Sciences Institute, Durham University, Durham, UK aut Rodgers Thomas Biophysical Sciences Institute, Durham University, Durham, UK aut Pohl Ehmke Biophysical Sciences Institute, Durham University, Durham, UK aut Wilson Mark Biophysical Sciences Institute, Durham University, Durham, UK aut McLeish Tom Biophysical Sciences Institute, Durham University, Durham, UK aut Cann Martin Biophysical Sciences Institute, Durham University, Durham, UK aut Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 175-182 1867-2450 7:2<175 2015 7 12551 https://doi.org/10.1007/s12551-015-0163-9 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s12551-015-0163-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Townsend Philip Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 700 1- Rodgers Thomas Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 700 1- Pohl Ehmke Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 700 1- Wilson Mark Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 700 1- McLeish Tom Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 700 1- Cann Martin Biophysical Sciences Institute, Durham University, Durham, UK aut NATIONALLICENCE 773 0- Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 175-182 1867-2450 7:2<175 2015 7 12551