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Green Fluorescent Protein (GFP): Applications, Structure, and Related Photophysical Behavior
- M. Zimmer
- 4 June 2002
Green fluorescent protein (GFP): applications, structure, and related photophysical behavior.
- M. Zimmer
- Chemistry, MedicineChemical reviews
- 2 February 2002
Activation of the A2A adenosine G-protein-coupled receptor by conformational selection
Direct observation of the conformational equilibria of ligand-dependent G-protein-coupled receptor and deduction of the underlying mechanisms of receptor activation will have wide-reaching implications for the understanding of the function of G- proteins in health and disease.
Site-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site.
- B. Branchini, R. Magyar, M. Murtiashaw, S. Anderson, M. Zimmer
- Chemistry, MedicineBiochemistry
- 14 October 1998
The results of photoinactivation and kinetic and bioluminescence studies with these proteins are consistent with His245 being the primary functional target of BPTC-catalyzed enzyme inactivation, and a structure-based interpretation of the role of 244HHGF247 in firefly biolumscence is provided.
Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain.
Evidence is provided that Lys443 and Lys529, located on opposite sides of the C-terminal domain and conserved in all firefly luciferases, are each essential for only one of the partial reactions of firefly bioluminescence, supporting the proposal that the superfamily enzymes may adopt two different conformations to catalyze the two half-reactions.
GFP: from jellyfish to the Nobel prize and beyond.
- M. Zimmer
- MedicineChemical Society reviews
- 21 September 2009
The path taken by this jellyfish protein to become one of the most useful tools in modern science and medicine is described.
Photophysics and Dihedral Freedom of the Chromophore in Yellow, Blue, and Green Fluorescent Protein
- Colleen M. Megley, Luisa A. Dickson, Scott L. Maddalo, Gabriel J. Chandler, M. Zimmer
- Chemistry, MedicineThe journal of physical chemistry. B
- 9 December 2008
Green fluorescent protein (GFP) and GFP-like fluorescent proteins owe their photophysical properties to an autocatalytically formed intrinsic chromophore, and the dihedral freedom of the systems studied increases in the inverse order to the quantum yield.
Function and structure of GFP-like proteins in the protein data bank.
- Wayne J-H Ong, Samuel Alvarez, +6 authors M. Zimmer
- Chemistry, MedicineMolecular bioSystems
- 1 April 2011
The lid residues are important to the function of GFP-like proteins, perhaps in protecting the chromophore or in β-barrel formation, and chromophoric deviations from planarity play an important role in determining the fluorescence quantum yield.
The influence of P‐light chain phosphorylation by myosin light chain kinase on the calcium sensitivity of chemically skinned heart fibres
An enhanced phosphorylation level of the P‐light chain catalyzed by Ca2+‐calmodulin‐dependent myosin light chain kinase (MLCK) increased significantly theCa2+ sensitivity of chemically skinned ventricular fibre bundles of the pig.
The calmodulin fraction responsible for contraction in an intestinal smooth muscle
Freeze‐dried fibers of smooth muscle from Taenia coli were used to determine the concentration of calmodulin responsible for contraction. About 10% of the total intracellular calmodulin (12.6 μmol/kg…