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View bacteriocin : Thuricin-S |
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| [Ref. 1] | PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY, STRAIN=HD198 Chehimi S., Delalande F., Sable S., Hajlaoui M.R., Van Dorsselaer A., Limam F., Pons A.M. "Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis.", Submitted (JAN-2006) to Swiss-Prot. |
| Sequence |
........10 ........20 | | DWTXWSXLVX AACSVELL |
Warning: Partial sequence.
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| Wheel representation |
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| Formula |
C78
H111
N17
O20
S1
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| Absent amino acids |
FGHIKMNPQRY |
| Common amino acids |
LX |
| Mass (Da) |
1987.2 |
| Net charge |
-2 |
| Isoelectric point |
3.55 |
| Basic residues |
0 |
| Acidic residues |
2 |
| Hydrophobic residues |
9 |
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| Polar residues |
4 |
| Aliphatic residues |
5 |
| Tiny residues |
4 |
| Boman Index |
7.5 |
| Hydropathy Index |
0.82 |
| Aliphatic Index |
108.33 |
| Instability Index |
22.17 (stable)
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| Half Life |
Mammalian : 1.1 hour
Yeast : 3 min
E. coli : >10 hour |
| Extinction Coefficient |
11000 M-1 cm-1 |
| Absorbance 280nm |
647.06 |
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Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.
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