Secondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00371-8/fullpdf
Reference33 articles.
1. Purification and molecular properties of 3 polypeptides released from a highly active O2 -evolving photosystem-II preparation by Tris-treatment
2. Nucleotide sequence of cDNA clones encoding the complete ‘23 kDa’ and ‘16 kDa’ precursor proteins associated with the photosynthetic oxygen-evolving complex from spinach
3. Complete amino acid sequence of 33 kDa protein isolated from spinach photosystem II particles
4. The extrinsic polypeptides of Photosystem II
5. Role of the 33-kDa polypeptide in preserving Mn in the photosynthetic oxygen-evolution system and its replacement by chloride ions
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1. Honey bee odorant-binding protein 14: effects on thermal stability upon odorant binding revealed by FT-IR spectroscopy and CD measurements;European Biophysics Journal;2013-12-21
2. FTIR Evidence That the PsbP Extrinsic Protein Induces Protein Conformational Changes around the Oxygen-Evolving Mn Cluster in Photosystem II;Biochemistry;2009-06-16
3. Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry;Vibrational Spectroscopy;2009-05
4. Tyrosine Residues of the Extrinsic 23 kDa Protein Are Important for Its Interaction with Spinach PSII Membranes;Protein & Peptide Letters;2006-06-01
5. Unfolding Features of Bovine Testicular Hyaluronidase Studied by Fluorescence Spectroscopy and Fourier Transformed Infrared Spectroscopy;Journal of Fluorescence;2005-11
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