Circular dichroism and fluorescence spectroscopic analyses of a proline-rich glycoprotein from human parotid saliva

2009 ◽  
Vol 26 (6) ◽  
pp. 621-629 ◽  
Author(s):  
RONALD E. LOOMIS ◽  
E. JAMES BERGEY ◽  
MICHAEL J. LEVINE ◽  
LAWRENCE A. TABAK
Keyword(s):  
Circular Dichroism ◽  
Parotid Saliva ◽  
Spectroscopic Analyses ◽  
Circular Dichroïsm ◽  
Human Parotid Saliva

scholarly journals Glycosylated proline-rich peptide of human parotid saliva. Circular dichroism study

FEBS Letters ◽  
1975 ◽  
Vol 56 (2) ◽  
pp. 263-267 ◽  
Author(s):  
J.P. Aubert ◽  
A. Boersma ◽  
M.H. Loucheux-Lefebvre ◽  
P. Degand ◽  
G. Biserte
Keyword(s):  
Circular Dichroism ◽  
Parotid Saliva ◽  
Proline Rich Peptide ◽  
Circular Dichroïsm ◽  
Human Parotid Saliva

Circular dichroism studies on the proline-rich glycoprotein of human parotid saliva

1982 ◽  
Vol 704 (2) ◽  
pp. 361-365 ◽  
Author(s):  
Jean-pierre Aubert ◽  
Nicole Porchet ◽  
Arnold Boersma ◽  
Marie-Henriette Loucheux-Lefebvre ◽  
Pierre Degand
Keyword(s):  
Circular Dichroism ◽  
Parotid Saliva ◽  
Circular Dichroïsm ◽  
Human Parotid Saliva

scholarly journals A Novel Azaphilone Muyophilone A From the Endophytic Fungus Muyocopron laterale 0307-2

2021 ◽  
Vol 9 ◽  
Author(s):  
Chao Yuan ◽  
Yuhua Guo ◽  
Ke Wang ◽  
Zhunian Wang ◽  
Longfei Li ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Nmr Spectroscopy ◽  
Single Crystal ◽  
Endophytic Fungus ◽  
Vibrational Circular Dichroism ◽  
Spectroscopic Methods ◽  
X Ray Diffraction ◽  
X Ray ◽  
Spectroscopic Analyses ◽  
Circular Dichroïsm

Two known azaphilone derivatives, 4,6-dimethylcurvulinic acid (1) and austdiol (2), and their novel heterotrimer, muyophilone A (3), were isolated and identified from an endophytic fungus, Muyocopron laterale 0307-2. Their structures and stereochemistry were established by extensive spectroscopic analyses including HRMS, NMR spectroscopy, electronic circular dichroism (ECD) and vibrational circular dichroism (VCD) spectroscopic methods, as well as single crystal X-ray diffraction. In the structure of 3, two compound 2-derived azaphilone units were connected through an unprecedented five-membered carbon bridge which was proposed to be originated from compound 1. Compound 3 represents the first example of azaphilone heterotrimers.

scholarly journals Aspidoptoids A–D: Four New Diterpenoids from Aspidopterys obcordata Vine

Molecules ◽  
2020 ◽  
Vol 25 (3) ◽  
pp. 529
Author(s):  
Sun ◽  
Cao ◽  
Xiao ◽  
Zhang ◽  
Wang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Circular Dichroism ◽  
Absolute Configuration ◽  
2D Nmr ◽  
Cytotoxic Activities ◽  
No Production ◽  
Inhibitory Effects ◽  
Electronic Circular Dichroism ◽  
Spectroscopic Analyses ◽  
Circular Dichroïsm

Four new diterpenoids, named aspidoptoids A–D (1–4), together with two known analogues (5–6) were isolated from Aspidopterys obcordata vine. Aspidoptoids A–B (1–2) are the first examples of phenylethylene-bearing 20-nor-diterpenoids of which aspidoptoid B (2) possesses a rare 3,10-oxybridge. Their structures and absolute configuration were determined by extensive spectroscopic analyses (IR, HRESIMS, 1D and 2D NMR) and electronic circular dichroism (ECD) calculation. In addition, all the isolates were evaluated for their cytotoxic activities and inhibitory effects on the nitric oxide (NO) production.

scholarly journals A New Diterpenoid with a Rearranged Skeleton from Salvia prattii

2017 ◽  
Vol 12 (8) ◽  
pp. 1934578X1701200
Author(s):  
Hiroshi Kawabe ◽  
Riyo Suzuki ◽  
Hiroshi Hirota ◽  
Keiichi Matsuzaki ◽  
Xun Gong ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Hela Cell ◽  
Cell Lines ◽  
Absolute Configuration ◽  
Electronic Circular Dichroism ◽  
Methyl Group ◽  
Spectroscopic Analyses ◽  
Hela Cell Lines ◽  
The Absolute ◽  
Circular Dichroïsm

A new diterpenoid with a rearranged skeleton, prattinin A (1), was isolated along with five known compounds (2–6) from the roots of Salvia prattii. The structure of 1 bearing a methyl group at the C-5 position was established by extensive spectroscopic analyses and the absolute configuration of 1 was elucidated by comparing the calculated and experimental electronic circular dichroism (ECD) spectra. Compounds 1, 3, 4, and 5 exhibited moderate or weak cytotoxicity against HL-60 and HeLa cell lines.

scholarly journals Structural Changes Revealed by Fourier Transform Infrared and Circular Dichroism Spectroscopic Analyses Underlie tNOX Periodic Oscillations

Dose-Response ◽  
2005 ◽  
Vol 3 (3) ◽  
pp. dose-response.0 ◽  
Author(s):  
Chinpal Kim ◽  
Sara Layman ◽  
Dorothy M. Morré ◽  
D. James Morré
Keyword(s):  
Fourier Transform ◽  
Circular Dichroism ◽  
Enzymatic Activity ◽  
Structural Changes ◽  
Deuterium Oxide ◽  
Fourier Transform Infrared ◽  
Period Length ◽  
Global Changes ◽  
Spectroscopic Analyses ◽  
Circular Dichroïsm

A recurring pattern of spectral changes indicative of periodic changes in the proportion of β-structure and a-helix of a recombinant ECTO-NOX fusion protein of tNOX, with a cellulose binding domain peptide, was demonstrated by Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopic analyses. The pattern of structural changes correlated with oscillatory patterns of enzymatic activities exhibited by the protein previously interpreted as indicative of a clock function. The pattern consisted of a repeating pattern of oscillations with a period length of 21 min with five maxima (two separated by 5 min and 3 separated by 4 to 4.5 min) within each 21 min repeat. Oscillatory patterns were not obvious in comparable FTIR or CD spectra of albumin, ribonuclease or concanavalin A. The period length was constant at 5, 15, 25, 35 and 45° C (temperature compensated) and oscillations occurred independently of substrate presence. Spectra obtained in deuterium oxide yielded a longer period length of 26 min both for oscillations in enzymatic activity and absorbance ratios determined by FTIR. Taken together the findings suggest that the regular patterns of oscillations exhibited by the ECTO-NOX proteins are accompanied by recurrent global changes in the conformation of the protein backbone that directly modulate enzymatic activity.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

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