Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1939359 | Biochemical and Biophysical Research Communications | 2006 | 5 Pages |
Abstract
Infrared and Raman spectroscopy were applied to identify restraints for the structure determination of the 20 amino acid loop between two β-sheets of the N-terminal region of the PsbQ protein of the oxygen evolving complex of photosystem II from Spinacia oleracea by restraint-based homology modeling. One of the initial models has shown a stable fold of the loop in a 20 ns molecular dynamics simulation that is in accordance with spectroscopic data. Cleavage of the first 12 amino acids leads to a permanent drift in the root means square deviation of the protein backbone and induces major structural changes.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Jaroslava Ristvejová, Vladimír Kopecký Jr., Žofie Sovová, Mónica Balsera, Juan B. Arellano, Michael Green, Rüdiger Ettrich,