scholarly journals Investigating the Structure and Dynamics of Apo‐Photosystem II

ChemCatChem ◽  
2019 ◽  
Vol 11 (16) ◽  
pp. 4072-4080 ◽  
Author(s):  
Ruocheng Han ◽  
Katharina Rempfer ◽  
Miao Zhang ◽  
Holger Dobbek ◽  
Athina Zouni ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Structure And Dynamics

Low-Energy Exciton Level Structure and Dynamics in LightHarvesting Complex II Trimers from the Chl a/b Antenna Complex of Photosystem II

1994 ◽  
Vol 98 (17) ◽  
pp. 4729-4735 ◽  
Author(s):  
N. R. S. Reddy ◽  
H. van Amerongen ◽  
S. L. S. Kwa ◽  
R. van Grondelle ◽  
G. J. Small
Keyword(s):  
Photosystem Ii ◽  
Level Structure ◽  
Low Energy ◽  
Complex Ii ◽  
Chl A ◽  
Structure And Dynamics ◽  
Antenna Complex

Structure and dynamics of the N-terminal loop of PsbQ from photosystem II of Spinacia oleracea

2006 ◽  
Vol 345 (1) ◽  
pp. 287-291 ◽  
Author(s):  
Jaroslava Ristvejová ◽  
Vladimír Kopecký ◽  
Žofie Sovová ◽  
Mónica Balsera ◽  
Juan B. Arellano ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Spinacia Oleracea ◽  
Structure And Dynamics ◽  
Terminal Loop

Corrigendum to “Structure and dynamics of the N-terminal loop of PsbQ from photosystem II of Spinacia oleracea” [Biochem. Biophys. Res. Commun. 345 (2006) 287–291]

2006 ◽  
Vol 348 (3) ◽  
pp. 1205
Author(s):  
Jaroslava Ristvejová ◽  
Vladimír Kopecký ◽  
Žofie Sovová ◽  
Mónica Balsera ◽  
Juan B. Arellano ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Spinacia Oleracea ◽  
Structure And Dynamics ◽  
Terminal Loop

scholarly journals Exciton Level Structure and Dynamics in the CP47 Antenna Complex of Photosystem II

1994 ◽  
Vol 98 (31) ◽  
pp. 7717-7724 ◽  
Author(s):  
H.-C. Chang ◽  
R. Jankowiak ◽  
C. F. Yocum ◽  
R. Picorel ◽  
M. Alfonso ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Level Structure ◽  
Structure And Dynamics ◽  
Antenna Complex

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

Nucleosome dynamics

2006 ◽  
Vol 73 ◽  
pp. 109-119 ◽  
Author(s):  
Chris Stockdale ◽  
Michael Bruno ◽  
Helder Ferreira ◽  
Elisa Garcia-Wilson ◽  
Nicola Wiechens ◽  
...  
Keyword(s):  
High Resolution ◽  
Chromatin Structure ◽  
Current Knowledge ◽  
Dynamic Properties ◽  
Structure And Dynamics ◽  
Nucleosome Dynamics ◽  
Sharp Focus ◽  
Recent Advances ◽  
Insight Into ◽  
Chromatin Structure And Dynamics

In the 30 years since the discovery of the nucleosome, our picture of it has come into sharp focus. The recent high-resolution structures have provided a wealth of insight into the function of the nucleosome, but they are inherently static. Our current knowledge of how nucleosomes can be reconfigured dynamically is at a much earlier stage. Here, recent advances in the understanding of chromatin structure and dynamics are highlighted. The ways in which different modes of nucleosome reconfiguration are likely to influence each other are discussed, and some of the factors likely to regulate the dynamic properties of nucleosomes are considered.

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