Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions

2011 ◽  
Vol 123 (16) ◽  
pp. 3839-3843 ◽  
Author(s):  
Loïc Salmon ◽  
José-Luis Ortega Roldan ◽  
Ewen Lescop ◽  
Antoine Licinio ◽  
Nico van Nuland ◽  
...  
Keyword(s):  
Spin Relaxation ◽  
Protein Complexes ◽  
Structure Dynamics ◽  
Relaxation Measurements ◽  
Nmr Spin Relaxation ◽  
Kinetics Of

Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions

2011 ◽  
Vol 50 (16) ◽  
pp. 3755-3759 ◽  
Author(s):  
Loïc Salmon ◽  
José-Luis Ortega Roldan ◽  
Ewen Lescop ◽  
Antoine Licinio ◽  
Nico van Nuland ◽  
...  
Keyword(s):  
Spin Relaxation ◽  
Protein Complexes ◽  
Structure Dynamics ◽  
Relaxation Measurements ◽  
Nmr Spin Relaxation ◽  
Kinetics Of

Muon-spin relaxation measurements of geometrically frustrated magnets

2001 ◽  
Vol 79 (11-12) ◽  
pp. 1295-1305 ◽  
Author(s):  
K M Kojima
Keyword(s):  
Spin Relaxation ◽  
Muon Spin ◽  
Muon Spin Relaxation ◽  
Spin Systems ◽  
Frustrated Magnets ◽  
Slow Dynamics ◽  
Kagomé Lattice ◽  
Geometrically Frustrated ◽  
Relaxation Measurements ◽  
Frustrated Spin

Muon-spin relaxation (µSR) has been applied to investigations of slow dynamics and quasi-static features of geometrically frustrated spin systems. We take an example in the Kagome-lattice anti-ferromagnets, and briefly review µSR works on S = 1, 3/2, and 5/2 Kagome compounds. PACS No.: 75.30

Long-range electron–electron interaction and charge transfer in protein complexes: a numerical approach

2019 ◽  
Vol 21 (34) ◽  
pp. 18595-18604 ◽  
Author(s):  
David Gnandt ◽  
Thorsten Koslowski
Keyword(s):  
Electron Transfer ◽  
Charge Transfer ◽  
Protein Complexes ◽  
Numerical Approach ◽  
Pair Approximation ◽  
Electron Interaction ◽  
Coulomb Interactions ◽  
Electron Transfer Proteins ◽  
Thermodynamics And Kinetics ◽  
Kinetics Of

Coulomb interactions in large electron transfer proteins can be addressed within a pair approximation. They have a profound effect on the thermodynamics and kinetics of charge transport.

The Influence of 5-Aminolevulinic Acid on Protochlorophyllide and Protochlorophyll Accumulation in Dark-Grown Scenedesmus

1990 ◽  
Vol 45 (1-2) ◽  
pp. 71-73 ◽  
Author(s):  
Kiriakos Kotzabasis ◽  
Horst Senger
Keyword(s):  
Aminolevulinic Acid ◽  
Protein Complexes ◽  
Chlorophyll Biosynthesis ◽  
Scenedesmus Obliquus ◽  
Good Tool ◽  
Future Studies ◽  
Pigment Protein Complexes ◽  
Kinetics Of ◽  
Grown Culture ◽  
In Cells

The intermediate of chlorophyll biosynthesis, 5-aminolevulinic acid (ALA ), is a necessary prerequisite for the formation of protochlorophyllide (PChlide) and protochlorophyll (PChl) in the dark. The application of ALA to a dark-grown culture of the pigment mutant C-2 A′ of Scenedesmus obliquus increased the amount of PChlide 30-fold and the amount of PChl about 10-fold. The rates of ALA-dependent formation of PChlide and PChl reach their maximum values at different concentrations of added ALA . Similarly, the kinetics of PChlide and PChl formation in cells incubated with ALA are different. Cells of Scenedesmus mutant C-2 A′ incubated with various concentrations of ALA for different periods provide a good tool for future studies differentiating between PChlide and PChl metabolism . − The incorporation of Chl deriving from either PChl or PChlide into different pigment protein complexes is discussed.

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