Secondary structure of ActA, N-ActA, P-ActA, and C-ActA in the absence or presence of phospholipid
Range | Table - link |
---|---|
Organism | Bacteria Listeria monocytogenes |
Reference | Cicchetti G, Maurer P, Wagener P, Kocks C. Actin and phosphoinositide binding by the ActA protein of the bacterial pathogen Listeria monocytogenes. J Biol Chem. 1999 Nov 19 274(47):33616-26. p.33622 table 2PubMed ID10559250 |
Method | Secondary structure calculations based on far UV-CD spectra between 186 and 250 nm were performed using the SELCON program with the dataset including 17 reference proteins. |
Entered by | Uri M |
ID | 106832 |