title: Protein conformation: through a lens, darkly.
abstract: This commentary describes the study by Calleja and co-workers, who have used fluorescence resonance energy transfer between two fluorescent proteins fused to one protein kinase (protein kinase B/Akt) to reveal conformational changes in a functional protein. The findings of their study offer an intriguing insight into the behaviour of an enzyme that is essential for multiple aspects of mammalian signalling.
authors.affiliation: School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK. R.H.Insall@bham.ac.uk
authors.forename: Robert
authors.initials: R
authors.lastname: Insall
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins / Q000737:chemistry; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D011518:Proto-Oncogene Proteins; D051057:Proto-Oncogene Proteins c-akt; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D008164:Luminescent Proteins; D011518:Proto-Oncogene Proteins; D011994:Recombinant Proteins; C054562:yellow fluorescent protein, Bacteria; D049452:Green Fluorescent Proteins; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt