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The guanidine hydrochloride-induced denaturation of CP43 and CP47 studied by terahertz time-domain spectroscopy

Science in China Series C: Life Sciences, 2007
Terahertz time-domain spectroscopy (THz-TDS) is a new technique in studying the conformational state of a molecule in recent years. In this work, we reported the first use of THz-TDS to examine the denaturation of two photosynthesis membrane proteins: CP43 and CP47.
YuanGang, Qu   +5 more
openaire   +2 more sources

Mutational Studies on Conserved Histidine Residues in the Chlorophyll‐Binding Protein CP43 of Photosystem II

European Journal of Biochemistry, 1997
Two chlorophyll‐binding antenna proteins in the photosystem II core, CP43 and CP47, are structurally similar and are thought to have evolved from a common ancestor. Several conserved histidine residues in hydrophobic regions of CP47 have been shown to be important for photosystem I1 structure, function, and energy transfer.
P, Manna, W, Vermaas
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Structure of the Cyanobacterial Photosystem II: An Indication of Different Functions of CP47 and CP43

1992
Photosystem II, a multicomponent chlorophyll-protein complex, is very labile and easily disintegrates during isolation and other manipulation at temperatures above 0° C. PSII preparations from thermophilic cyanobacteria are characterized by a higher stability and, therefore, they are a suitable object for structural and functional studies. Zwitterionic
Josef Komenda   +2 more
openaire   +1 more source

Thermal denaturation of CP43 studied by Fourier transform-infrared spectroscopy and terahertz time-domain spectroscopy

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007
Thermal denaturation of CP43 was studied by Fourier transform-infrared (FT-IR) spectroscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and terahertz time-domain spectroscopy (THz-TDS). Under heat treatment, the secondary structure of CP43 changed, and the main thermal transition occurred at 59 degrees C.
Yuangang, Qu   +5 more
openaire   +2 more sources

Purification and Characterization of the Core Antenna CP43 of Photosystem II.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica
The core antenna CP43 of photosystem II was purified from the PSII core complex of spinach by DEAE-Toyopearl-650S anion-exchange chromatography, using the mild nonionic detergent beta-dodecyl maltoside and high concentration of LiClO(4). At room temperature, the purified CP43 has a maximum absorption at 671 nm, a fluorescence maximum at 683 nm and ...
Xiao-Peng, Liu   +2 more
openaire   +1 more source

Unfolding of apo-CP43 Induced by Guanidine Hydrochloride

Chinese Journal of Applied and Environmental Biology, 2012
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Light- and heat-induced denaturation of photosystem II core-antenna complexes CP43 and CP47

Journal of Photochemistry and Photobiology B: Biology, 1999
Tingyun Kuang   +2 more
exaly  

Spectroscopic study of trypsin, heat and Triton X-100-induced denaturation of the chlorophyll-binding protein CP43

Journal of Photochemistry and Photobiology B: Biology, 2000
Tingyun Kuang   +2 more
exaly  

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