Intermolecular β-Sheet Results from Trifluoroethanol-Induced Nonnative α-Helical Structure in β-Sheet Predominant Proteins: Infrared and Circular Dichroism Spectroscopic Study

1998 ◽  
Vol 355 (2) ◽  
pp. 275-281 ◽  
Author(s):  
Aichun Dong ◽  
James Matsuura ◽  
Mark C. Manning ◽  
John F. Carpenter
Keyword(s):  
Circular Dichroism ◽  
Spectroscopic Study ◽  
Helical Structure ◽  
Circular Dichroïsm ◽  
Β Sheet

scholarly journals A Raman, SERS and UV-circular dichroism spectroscopic study of N-acetyl-l-cysteine in aqueous solutions

2019 ◽  
Vol 43 (38) ◽  
pp. 15201-15212 ◽  
Author(s):  
R. A. Cobos Picot ◽  
M. Puiatti ◽  
A. Ben Altabef ◽  
R. J. G. Rubira ◽  
S. Sanchez-Cortes ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Circular Dichroism ◽  
Aqueous Solutions ◽  
Spectroscopic Study ◽  
Electronic Properties ◽  
Structural Properties ◽  
Amine Groups ◽  
Circular Dichroïsm

The aim of this work is to evaluate the vibrational and structural properties of N-acetyl-l-cysteine (NAC), and its molecular structure and electronic properties in relation to the action of thiol and amine groups at different pH.

Helical structure of sugar-carrying polystyrene in aqueous solution by circular dichroism

2003 ◽  
Vol 338 (20) ◽  
pp. 2129-2133 ◽  
Author(s):  
Shojiro Shimojo ◽  
Chong-Su Cho ◽  
In-Kyu Park ◽  
Megumi Kunou ◽  
Mitsuaki Goto ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Circular Dichroism ◽  
Helical Structure ◽  
Circular Dichroïsm

Preparation of Polypeptide-Dye Multilayers by an Electrostatic Assembly Process

1994 ◽  
Vol 351 ◽  
Author(s):  
Thomas M. Cooper ◽  
L. Campbell Angela ◽  
Carol Noffsinger ◽  
Janelle Gunther-Greer ◽  
Robert L. Crane ◽  
...  
Keyword(s):  
Thin Films ◽  
Circular Dichroism ◽  
Glutamic Acid ◽  
Congo Red ◽  
Copper Phthalocyanine ◽  
Electrostatic Assembly ◽  
Amino Silane ◽  
Spectrum Characteristic ◽  
Circular Dichroïsm ◽  
Β Sheet

ABSTRACTTo develop novel optical thin films, we have prepared self-assembled polypeptide films by an electrostatic process. The films were placed on a glass slide previously silanized by an amino silane and given a positive charge by immersion in aqueous acid. Subsequent immersion of the slide in aqueous anionic solutions of either poly(L-glutamic acid), congo red, copper phthalocyanine tetrasulfonic acid or p-nitroaniline-modified poly(L-glutamic acid) resulted in deposition of the anions on the surface. Following anionic immersion, the slides were dipped into a cationic poly(L-lysine) solution. Alternate dipping into anionic and cationic solutions yielded multilayers. The thin films were characterized by optical absorption and circular dichroism. The optical density increased with dipping cycles. Circular dichroism measurements of the thin films showed induced dichroism of the congo red and phthalocyanine-containing films, suggesting formation of a locally ordered dye-polypeptide complex. Solution circular dichroism measurements of the polypeptides indicated a coil conformation, while poly(Lglutamic acid)/poly(L-lysine) complexes showed circular dichroism spectrum characteristic of a β-sheet.

Germin: physicochemical properties of the glycoprotein which signals onset of growth in the germinating wheat embryo

1987 ◽  
Vol 65 (12) ◽  
pp. 1039-1048 ◽  
Author(s):  
William C. McCubbin ◽  
Cyril M. Kay ◽  
Theresa D. Kennedy ◽  
Byron G. Lane
Keyword(s):  
Circular Dichroism ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Helical Structure ◽  
Random Coil ◽  
Sedimentation Equilibrium ◽  
Cross Linking ◽  
Wheat Embryo ◽  
Circular Dichroïsm

The size and structure of germin, the homooligomeric glycoprotein which marks the onset of growth in germinating wheat embryos, has been examined by gel filtration, ultracentrifugation, electron microscopy, chemical cross-linking, and optical techniques (circular dichroism). Germin has a sedimentation coefficient (S20,w) of 7.3S, and a Stokes' radius (RS) of 4.5 nm, the latter value being compatible with the dimensions of the particle observed by negative staining in the electron microscope. By three methods (sedimentation equilibrium, sodium dodecyl sulphate (SDS) – polyacrylamide electrophoresis, S20,w/RS), the mean particle mass of the two closely related forms of germin (G and G′) is ca. 130 kilodaltons (kDa). Cross-linking with dimethyl suberimidate indicates that the oligomer is homopentameric, compatible with the molecular mass of the protomer (ca. 26 kDa) as determined by SDS–polyacrylamide gel electrophoresis. Using the Provencher and Glockner analysis to interpret circular dichroism measurements (in the far ultraviolet), both forms of germin contain about 10–20% α-helical structure, 50–60% β-sheet/turn structure, and 20–30% random coil. In a structure-inducing environment (45% trifluoroethanol), the α-helical structure increases to a value (35–40%) similar to that predicted by Chou–Fasman analysis of the protein sequence deduced by cDNA sequencing.

scholarly journals Conformational studies of biliproteins from the insects pieris brassicae and cerura vinula

1988 ◽  
Vol 43 (1-2) ◽  
pp. 84-90 ◽  
Author(s):  
Hugo Scheer ◽  
Hartmut Kayser
Keyword(s):  
Circular Dichroism ◽  
Optical Activity ◽  
Fluorescence Spectra ◽  
Protein A ◽  
Protein Secondary Structure ◽  
Helical Structure ◽  
Pieris Brassicae ◽  
Bile Pigments ◽  
Urea Denaturation ◽  
Circular Dichroïsm

Chromophore conformation and protein secondary structure of biliproteins from the butterfly, Pieris brassicae, and the moth, Cerura vinula, have been investigated by absorption, circular dichroism and fluorescence spectroscopy. The chromophore of the P. brassicae protein, biliverdin IXy, has probably a cyclic-helical structure similar to that of free bile pigments of the biliverdin type. Though achiral by structure the chromophore displays strong optical activity in the native protein-bound state, but becomes inactive after urea denaturation of the protein. A minor biliprotein from P. brassicae shows absorption, circular dichroism and fluorescence spectra identical to the main biliprotein. In the biliprotein from Cerura vinula the structure of the pigment is still unknown. It has a semi-open conformation intermediate between that of the Pieris proteins and that of the phycobiliprotein, C-phycocyanin, and it retains optical activity after urea denaturation. The band widths and the size of the Stokes shifts of the fluorescence spectra indicate a high degree of conformational flexibility of the chromophores in the two Pieris pigments, and a decreased flexibility in the one from Cerura. In the biliproteins from both insects the polypeptides are low in a-helix content compared to that of phycobiliproteins. From these and earlier data, insect and algal biliproteins seem to be related only distantly if at all, but there exist also considerable differences among insect biliproteins from different species

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