Unique conformational properties of muscle carbonic anhydrase III as demonstrated by circular dichroism spectrometry

Biochemistry ◽  
1979 ◽  
Vol 18 (2) ◽  
pp. 343-348 ◽  
Author(s):  
Martha K. Koester ◽  
Ernst A. Noltmann
Keyword(s):  
Circular Dichroism ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Conformational Properties ◽  
Circular Dichroism Spectrometry ◽  
Circular Dichroïsm

Circular dichroism and fluorescence studies to probe the conformational properties of Rhus vernicifera laccase

1992 ◽  
Vol 193 (2) ◽  
pp. 237-243 ◽  
Author(s):  
Fernanda Ricchelli ◽  
Mariano Beltramini ◽  
Luigi Bubacco ◽  
Benedetto Salvato ◽  
Bruno Filippi
Keyword(s):  
Circular Dichroism ◽  
Fluorescence Studies ◽  
Conformational Properties ◽  
Rhus Vernicifera ◽  
Circular Dichroïsm

Circular dichroism and the conformational properties of soybean β-amylase

1981 ◽  
Vol 211 (1) ◽  
pp. 382-389 ◽  
Author(s):  
Eigo Mori ◽  
Bunzo Mikami ◽  
Yuhei Morita ◽  
Bruno Jirgensons
Keyword(s):  
Circular Dichroism ◽  
Conformational Properties ◽  
Circular Dichroïsm

Circular dichroism and conformational properties of modeccin, a toxic protein

1983 ◽  
Vol 2 (2) ◽  
pp. 105-111 ◽  
Author(s):  
Bruno Jirgensons ◽  
George R. Bousfield ◽  
William T. Moore
Keyword(s):  
Circular Dichroism ◽  
Toxic Protein ◽  
Conformational Properties ◽  
Circular Dichroïsm

scholarly journals The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1646 ◽  
Author(s):  
Mattia Di Gaspero ◽  
Paolo Ruzza ◽  
Rohanah Hussain ◽  
Claudia Honisch ◽  
Barbara Biondi ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Antioxidant Properties ◽  
White Wine ◽  
Cd Spectra ◽  
Wine Quality ◽  
Melting Temperatures ◽  
Conformational Properties ◽  
Circular Dichroïsm ◽  
Important Constituent

Polyphenols are an important constituent of wines and they are largely studied due to their antioxidant properties and for their effects on wine quality and stability, which is also related to their capacity to bind to proteins. The effects of some selected polyphenols, including procyanidins B1 and B2, tannic acid, quercetin, and rutin, as well as those of a total white wine procyanidin extract on the conformational properties of the major wine protein VVTL1 (Vitis vinifera Thaumatin-Like-1) were investigated by Synchrotron Radiation Circular Dichroism (SRCD). Results showed that VVTL1 interacts with polyphenols as demonstrated by the changes in the secondary (far-UV) and tertiary (near-UV) structures, which were differently affected by different polyphenols. Additionally, polyphenols modified the two melting temperatures (TM) that were found for VVTL1 (32.2 °C and 53.9 °C for the protein alone). The circular dichroism (CD) spectra in the near-UV region revealed an involvement of the aromatic side-chains of the protein in the interaction with phenolics. The data demonstrate the existence of an interaction between polyphenols and VVTL1, which results in modification of its thermal and UV denaturation pattern. This information can be useful in understanding the behavior of wine proteins in presence of polyphenols, thus giving new insights on the phenomena that are involved in wine stability.

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