The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein (2015)
Journal Article
Townsend, P., Rodgers, T., Glover, L., Korhonen, H., Richards, S., Colwell, L., …Cann, M. (2015). The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein. Journal of Biological Chemistry, 290(36), 22225-22235. https://doi.org/10.1074/jbc.m115.669267

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. Both experimental and theoretical evidence demonstrate that allostery can be communicated through altered slow relaxation protein dynamics... Read More about The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein.

Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors (2013)
Journal Article
Rodgers, T., Townsend, P., Burnell, D., Jones, M., Richards, S., McLeish, T., …Cann, M. (2013). Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors. PLoS Biology, 11(9), Article e1001651. https://doi.org/10.1371/journal.pbio.1001651

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distinct site. There is growing evidence that allosteric cooperativity can be communicated by modulation of protein dynamics without conformational chang... Read More about Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors.