Exciton interaction in the photosystem I reaction center from spinach chloroplasts. Absorption and circular dichroism difference spectra

Biochemistry ◽  
1972 ◽  
Vol 11 (24) ◽  
pp. 4591-4595 ◽  
Author(s):  
Kenneth D. Philipson ◽  
Vicki L. Sato ◽  
Kenneth Sauer
Keyword(s):  
Circular Dichroism ◽  
Reaction Center ◽  
Photosystem I ◽  
Difference Spectra ◽  
Exciton Interaction ◽  
Spinach Chloroplasts ◽  
Circular Dichroïsm

Variability of light-induced circular dichroism spectra of photosystem I complexes of cyanobacteria

2010 ◽  
Vol 46 (3) ◽  
pp. 274-281 ◽  
Author(s):  
V. V. Shubin ◽  
M. Roegner ◽  
E. El-Mohsnawy ◽  
I. V. Terekhova ◽  
E. Schlodder ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Photosystem I ◽  
Induced Circular Dichroism ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm ◽  
Induced Circular Dichroism Spectra

Assignment of lectins specific for D-galactose or N-acetyl-D-galactosamine to two groups, based on their circular dichroism

1985 ◽  
Vol 63 (4) ◽  
pp. 268-271 ◽  
Author(s):  
N. Martin Young ◽  
Ross E. Williams
Keyword(s):  
Circular Dichroism ◽  
Ultraviolet Region ◽  
Cd Spectra ◽  
Difference Spectra ◽  
Sophora Japonica ◽  
Vicia Villosa ◽  
Near Ultraviolet ◽  
Caragana Arborescens ◽  
Wisteria Floribunda ◽  
Circular Dichroïsm

The circular dichroism (CD) spectra of thirteen lectins, most being specific for D-galactose or N-acetyl-D-galactosamine, were compared. Two groupings are proposed on the basis of the CD in the near-ultraviolet region. Group one comprises the lectins from Arachis hypogaea, Glycine max, Phaseolus coccineus, P. lunatus, P. vulgaris, and Vicia villosa, and group two comprises lectins from Caragana arborescens, Cytisus sessilifolius, Dolichos biflorus, Griffonia simplicifolia, and Wisteria floribunda. The CD spectra of lectins from Bauhinia purpurea and Sophora japonica were different from any of the other lectins. CD difference spectra produced by the two sugars were distinctive for each protein, suggesting that the combining sites of these lectins are not homologous despite similarities in specificity and that the CD spectral similarities arise from residues in other, more homologous regions of the proteins.

Conformation and orientation of chlorophyll-proteins in photosystem I by circular dichroism and polarized infrared spectroscopies

1984 ◽  
Vol 767 (3) ◽  
pp. 640-647 ◽  
Author(s):  
Eliane Nabedryk ◽  
Paule Biaudet ◽  
Sylvia Darr ◽  
Charles J. Arntzen ◽  
Jacques Breton
Keyword(s):  
Circular Dichroism ◽  
Photosystem I ◽  
Circular Dichroïsm

Nature of ligand affinity and dimerization of corticotrophin-releasing factor-binding protein may be detected by circular dichroism

1996 ◽  
Vol 16 (1) ◽  
pp. 39-44 ◽  
Author(s):  
P J Lowry ◽  
S C Koerber ◽  
R J Woods ◽  
S Baigent ◽  
S Sutton ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Binding Protein ◽  
Difference Spectra ◽  
Ligand Affinity ◽  
Corticotrophin Releasing Factor ◽  
Negative Change ◽  
Α Helix ◽  
Natural Peptides ◽  
Circular Dichroïsm ◽  
Β Sheet

ABSTRACT As the association of corticotrophin-releasing factor (CRF) with its binding protein (BP) to form a dimer complex (CRF2/BP2) appears to be dependent on the nature of the ligand we have compared the circular dichroism difference spectra after association of the BP with ovine (o) CRF, human (h) CRF and the α-helical CRF(9–41) antagonist. All three ligands caused a negative change in molar ellipticity above 210 nm, with oCRF having the least and hCRF the greatest effect. Below 210 nm there was a marked divergence of difference spectra, with the reaction with the natural peptides, hCRF and oCRF, resulting in a positive change in ellipticity, whilst that with the antagonist produced a negative change. In view of the BP spectrum indicating predominantly β-sheet and the peptides showing mainly α-helix these results were interpreted as the changes above 210 nm being due to dimerization and below 210 nm to a change in the conformation of ligand on binding. The opposite change in α-helicity of the antagonist observed on binding compared with the two natural CRF peptides could have fundamental pharmacological implications.

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