The Trimethylamine–Formic Acid Complex: Microwave Characterization of a Prototype for Potential Precursors to Atmospheric Aerosol

2016 ◽  
Vol 120 (14) ◽  
pp. 2268-2273 ◽  
Author(s):  
Rebecca B. Mackenzie ◽  
Christopher T. Dewberry ◽  
Kenneth R. Leopold
2019 ◽  
Vol 78 (18) ◽  
pp. 1651-1657
Author(s):  
Alexey Gubin ◽  
A. A. Lavrinovich ◽  
I. А. Protsenko ◽  
A. A. Barannik ◽  
S. Vitusevich

PIERS Online ◽  
2008 ◽  
Vol 4 (6) ◽  
pp. 686-690 ◽  
Author(s):  
Stepan Lucyszyn

IEEE Access ◽  
2021 ◽  
pp. 1-1
Author(s):  
Enrique Marquez-Segura ◽  
Sang-Hee Shin ◽  
Attique Dawood ◽  
Nick Ridler ◽  
Stepan Lucyszyn

1978 ◽  
Vol 173 (1) ◽  
pp. 237-243 ◽  
Author(s):  
M Isles ◽  
A R Foweraker ◽  
B R Jennings ◽  
T Hardingham ◽  
H Muir

An electric field causes partial alignment of macromolecules in a dilute solution. The accompanying changes in the solution birefringence offer a sensitive and quick means of monitoring the rates of particle orientation and hence the size of the solute molecules. Such measurements are reported for dilute solutions of proteoglycans in the absence and presence of added hyaluronic acid. The proteoglycan molecules are shown to be some 580 nm long. In the presence of hyaluronic acid they form aggregates that appear to be consistent with the model previously proposed in which the proteoglycans attach radially to the extended hyaluronic acid chain. The electric-birefringence relaxation rates indicate aggregates of similar length to that of the extended hyaluronic acid chain, with the proteoglycans spaced on average at 29nm intervals. A proteoglycan sample the cystine residues of which had been reduced and alkylated showed no evidence of aggregation with hyaluronic acid up to the concentrations of the acid corresponding to 1% of the total uronic acid content. The electric-birefringence method is shown to have a large potential in the study of associating polysaccharide solutions.


1988 ◽  
Vol 19 (7) ◽  
pp. 1215-1218 ◽  
Author(s):  
Bengt G. Martinsson ◽  
Hans-Christen Hansson

Author(s):  
G. Beaven ◽  
A. Bowyer ◽  
P. Erskine ◽  
S. P. Wood ◽  
A. McCoy ◽  
...  

The enzyme 2,4′-dihydroxyacetophenone dioxygenase (or DAD) catalyses the conversion of 2,4′-dihydroxyacetophenone to 4-hydroxybenzoic acid and formic acid with the incorporation of molecular oxygen. Whilst the vast majority of dioxygenases cleave within the aromatic ring of the substrate, DAD is very unusual in that it is involved in C—C bond cleavage in a substituent of the aromatic ring. There is evidence that the enzyme is a homotetramer of 20.3 kDa subunits each containing nonhaem iron and its sequence suggests that it belongs to the cupin family of dioxygenases. By the use of limited chymotrypsinolysis, the DAD enzyme fromAlcaligenessp. 4HAP has been crystallized in a form that diffracts synchrotron radiation to a resolution of 2.2 Å.


2006 ◽  
Vol 35 (6) ◽  
pp. 350-353
Author(s):  
P. A. Borodovskii ◽  
A. F. Buldygin ◽  
A. T. Drofa ◽  
A. S. Tokarev

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