scholarly journals The development of the intense circular-dichroic signal during granum formation in greening etiolated maize

1976 ◽  
Vol 156 (2) ◽  
pp. 469-472 ◽  
Author(s):  
S Demeter ◽  
L Mustardy ◽  
E Machowicz
Keyword(s):  
Circular Dichroism ◽  
Electron Micrographs ◽  
Early Formation ◽  
Membrane Contact ◽  
Circular Dichroïsm ◽  
Circular Dichroic

In greening maize mesophyll, circular dichroism (c.d.) revealed the early formation of protein-chlorophyll complexes, followed by unorganized chlorophyll. The intense c.d. [Gregory & Raps (1974) Biochem. J. 142, 193-201] appeared later still, whereas membrane-membrane contact (stacking), measured from electron micrographs, appeared much earlier. Isolated grana, which still showed stacking, lost 92% of their original intense c.d.; intense c.d. is not therefore simply dependent on stacking.

Organic photodiodes from homochiral l-proline derived squaraine compounds with strong circular dichroism

2017 ◽  
Vol 19 (10) ◽  
pp. 6996-7008 ◽  
Author(s):  
Matthias Schulz ◽  
Majvor Mack ◽  
Oliver Kolloge ◽  
Arne Lützen ◽  
Manuela Schiek
Keyword(s):  
Circular Dichroism ◽  
Polarized Light ◽  
Active Layers ◽  
Circular Dichroïsm ◽  
Circular Dichroic ◽  
Circular Polarized Light

We demonstrate the feasibility of inserting highly circular dichroic active layers into an organic photodiode as a potential detector for circular polarized light.

Circular dichroism of helical polynucleotide chains

1967 ◽  
Vol 297 (1448) ◽  
pp. 150-162 ◽  
Keyword(s):  
Circular Dichroism ◽  
Nucleic Acids ◽  
Helical Structure ◽  
Optical Rotatory Dispersion ◽  
Random Coil ◽  
Helical Conformation ◽  
Polyadenylic Acid ◽  
V Region ◽  
Circular Dichroïsm ◽  
Circular Dichroic

In contrast to relatively well developed experimental and theoretical studies on polypeptides and proteins (see Gratzer 1967 and McLachlan 1967, this volume) the investigation of optical activity of polynucleotides and nucleic acids were very restricted. The optical rotatory dispersion curves of polynucleotides examined in the visible and near u. v. fit one-term Drude equation regardless of the conformation (Fresco 1961; Levedahl & James 1957; Ts’o, Helmkamp & Sander 1962). Recent circular dichroism (c. d.) measurements of several polynucleotides and nucleic acids (figure 1) indicated clearly the presence of dichroic bands in the u. v. region of base absorption which can be related to the dissymmetrical helical conformation (Brahms 1963). The intensity of circular dichroic bands decreases strongly under the conditions in which the helical structure is unstable and goes to random coil form (Brahms 1964; Brahms & Mommaerts 1964). Thus polyadenylic acid (poly A ) is known according to X-ray data to exist at acid pH in a helical two strand and right handed conformation (Rich, Davies, Crick & Watson 1961). In acid solution the same polyadenylic acid exhibits strong circular dichroic bands which disappear at high temperature (figure 2).

scholarly journals Au Nanospirals Transferred onto PDMS Film Exhibiting Circular Dichroism at Visible Wavelengths

Micromachines ◽  
2020 ◽  
Vol 11 (7) ◽  
pp. 641
Author(s):  
Gaku Furusawa ◽  
Tetsuo Kan
Keyword(s):  
Thin Film ◽  
Circular Dichroism ◽  
Glancing Angle Deposition ◽  
Pdms Film ◽  
Glancing Angle ◽  
Dichroic Filter ◽  
Visible Wavelengths ◽  
Circular Dichroïsm ◽  
Circular Dichroic ◽  
Angle Deposition

We propose a thin, single-layered circular dichroic filter with Au nanospiral structures on a polydimethylsiloxane (PDMS) thin film that has strong circular dichroism at visible wavelengths. Au nanospiral structures with a diameter of 70 nm were fabricated by cryogenic glancing angle deposition on a substrate with a nanodot array template patterned with the block copolymer PS-PDMS. The Au nanospiral structures were transferred onto a transparent and flexible PDMS thin film to fabricate a thin, single-layered circular dichroic filter. The filter had a very large circular dichroism peak of −830 mdeg at 630 nm. The results show that the Au nanospiral structures transferred onto PDMS thin film exhibit large circular dichroism at visible wavelengths.

Linear oligopeptides. XXVII. Contribution to the circular dichroism of internal peptide chromophores

1976 ◽  
Vol 54 (1) ◽  
pp. 70-76 ◽  
Author(s):  
Claudio Toniolo ◽  
Gian Maria Bonora
Keyword(s):  
Circular Dichroism ◽  
Solvent Polarity ◽  
Guanidinium Chloride ◽  
Negative Band ◽  
Circular Dichroic Spectrum ◽  
Internal Peptide ◽  
Circular Dichroïsm ◽  
Sulfur Containing ◽  
Circular Dichroic ◽  
Molar Ellipticity

The contribution to the circular dichroism of L-Ala-L-Ala, L-Nva-L-Nva, L-Val-L-Val, L-Leu-L-Leu, L-Ile-L-Ile, L-Cys(Me)-L-Cys(Me), L-Met-L-Met, and L-Phe-L-Phe internal peptide chromophores in 1,1,1,3,3,3-hexafluoropropan-2-ol were calculated by subtracting the total molar ellipticity values of N- and C-protected homo-trimers from those of the pertinent protected homo-tetramers.The circular dichroism of the internal peptide chromophore of aliphatic hydrocarbon- and sulfur-containing peptides, each of the L-configuration, show a negative band at 2l5–230 nm accompanied by a more intense negative band near 200 nm. A structured weak and negative band near 260 nm along with bands at 240 nm (negative), 222 nm (positive), and 210.5 nm (negative) of progressively increasing intensity are apparent in the circular dichroic spectrum of L-Phe-L-Phe internal peptide chromophore. The effect of solvent polarity is discussed in the case of L-Val-L-Val and L-Ala-L-Ala internal peptide chromophores.Among the protected homo-trimers and tetramers only those of L-alanine are soluble in aqueous solution; consequently, the effect of water as a function of temperature, urea, and guanidinium chloride on the L-Ala-L-Ala internal peptide chromophore circular dichroism was established.

Water-soluble lysine-containing polypeptides. III. Sequential lysine-glycine polypeptides. A circular dichroism and electron microscopy study of annealed complexes with DNA, sonicated DNA, and denatured DNA

1976 ◽  
Vol 54 (24) ◽  
pp. 3884-3894 ◽  
Author(s):  
Sandra L. Kielland ◽  
Ross E. Williams
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Electron Micrographs ◽  
Microscopy Study ◽  
Electron Microscopy Study ◽  
Water Soluble ◽  
Size And Shape ◽  
Hydrophobic Nature ◽  
Circular Dichroïsm ◽  
Circular Dichroic

Circular dichroic spectra, turbidity measurements, and electron micrographs have been taken of annealled complexes of native, sonicated, and denatured DNA's in association with several sequential lysine-glycine copolypeptides. The results indicate that: (1) the molecular weight and strandedness of the DNA influences not only the assymmetric organization of the DNA in the complexes but also the size and shape of the complexes formed; (2) the hydrophobic nature (or sequence) of the polypeptide influences the shape of the complexes formed.

Water-soluble lysine-containing polypeptides. V. Circular dichroisrm, electron microscopic, and thermal denaturation studies of the interaction of poly(L-lysyl-L-alanine) and poly(L-lysyl-D-alanine) with calf thymus DNA

1978 ◽  
Vol 56 (20) ◽  
pp. 2650-2656 ◽  
Author(s):  
Sandra L. Kielland ◽  
Lewis A. Slotin ◽  
Ross E. Williams
Keyword(s):  
Circular Dichroism ◽  
Secondary Structure ◽  
Electron Micrographs ◽  
Thermal Denaturation ◽  
Water Soluble ◽  
Calf Thymus Dna ◽  
Circular Dichroism Spectra ◽  
Electron Microscopic ◽  
Calf Thymus ◽  
Circular Dichroïsm

Turbidity measurements, circular dichroism spectra, electron micrographs and thermal denaturation profiles of complexes between sonicated DNA and either poly(L-lysyl-L-alanine) or poly(L-lysyl-D-alanine) show significant differences which might be related to the primary or secondary structure of the polypeptides.

scholarly journals The nature of the circular-dichoric spectra of complexes between ribonuclease A and nucleotides

1977 ◽  
Vol 167 (3) ◽  
pp. 749-757 ◽  
Author(s):  
S M Dudkin ◽  
L V Karabashyan ◽  
M Y Karpeisky ◽  
S N Mikhailov ◽  
N S Padyukova ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Ribonuclease A ◽  
Circular Dichroic Spectrum ◽  
Nucleotide Conformation ◽  
Anti Conformation ◽  
Two Factors ◽  
Wavelength Absorption ◽  
Comparison Of The Results ◽  
Circular Dichroïsm ◽  
Circular Dichroic

The circular-dichroism and proton-magnetic-resonance spectra of complexes of ribonuclease A with dihydrouridine 3′-phosphate, 2′- and 3′-CMP, arabinosyl-3′-CMP, 1-(2-hydroxyethyl)cytosine 2′-phosphate and 1-(3-hydroxypropyl)cytosine 3′-phosphate were studied. Comparison of the results shows that non-additivity of the circular-dichroic spectrum of an enzyme-nucleotide complex may be due to: (a), alteration of the circular dichroic spectrum of the nucleotide under the influence of the asymmetric protein matrix (induced dichroism), and (b) a change in the nucleotide conformation. The contribution of each of the two factors was estimated to calculate the circular-dichoroic spectra of 2′-CMP and 3′-CMP in complex with ribonuclease A. 3′-CMP in this complex was characterized by negative circular dichroism in the long-wavelength absorption band of the nucleotide, whereas 2′-CMP was characterized by positive circular dichroism. Since both nucleotides in the complex are known to be in an anti conformation, it follows that even small changes in the conformation considerably modify the circular-dichroic spectrum of the nucleotide in complex with the enzyme.

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