Part:BBa_K2113005
AMP with glycine
This part contains the anti-microbial peptides (AMP) with consecutive sequences of arginine and tryptophan.These peptides have antimicrobial activity against wide range of microbes. In order to increase the shelf life and stability of the peptide glycine residues are added at the N terminal(GGWRWRWR).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Mobyl@RPBS
3D structural view
ProtParam Results(Physical and Chemical Properties)
Number of amino acids: 9
Molecular weight: 1290.51
Theoretical pI: 12.30
Total number of negatively charged residues (Asp + Glu): 0
Total number of positively charged residues (Arg + Lys): 3
Atomic composition:
Carbon (C): 60
Hydrogen (H): 83
Nitrogen (N): 21
Oxygen (O): 10
Sulfur (S): 1
Formula: C60H83N21O10S1
Total number of atoms: 175
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient: 16500
Abs 0.1% (=1 g/l): 12.786
Estimated half-life:
The N-terminal of the sequence considered is M (Met).
The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro).
>20 hours (yeast, in vivo).
>10 hours (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 163.60
This classifies the protein as unstable.
Aliphatic index: 0.00
Grand average of hydropathicity (GRAVY): -1.678
ExPASy Peptide Cutter Results
The following enzymes cleave this peptide.
| Name of enzyme | No. of cleavages | Positions of cleavage sites |
|---|---|---|
| Arg-C proteinase | 3 | 5 7 9 |
| BNPS-Skatole | 3 | 4 6 8 |
| CNBr | 1 | 1 |
| Chymotrypsin-high specificity (C-term to [FYW], not before P) | 3 | 4 6 8 |
| Chymotrypsin-low specificity (C-term to [FYWML], not before P) | 4 | 1 4 6 8 |
| Clostripain | 3 | 5 7 9 |
| Iodosobenzoic acid | 3 | 4 6 8 |
| Pepsin (pH>2) | 4 | 3 4 6 8 |
| Proteinase K | 3 | 4 6 8 |
| Trypsin | 3 | 5 7 9 |
These enzymes do not cut the peptide:
Asp-N endopeptidase
Asp-N endopeptidase + N-terminal Glu
Caspase1
Caspase10
Caspase2
Caspase3
Caspase4
Caspase5
Caspase6
Caspase7
Caspase8
Caspase9
Enterokinase
Factor Xa
Formic acid
Glutamyl endopeptidase
GranzymeB
Hydroxylamine
LysC
LysN
NTCB (2-nitro-5-thiocyanobenzoic acid)
Pepsin (pH1.3)
Proline-endopeptidase
Staphylococcal peptidase I
Thermolysin
Thrombin
Tobacco etch virus protease
References
1. Ressource Parisienne en Bioinformatique Structurale.(Mobyl@RPBS)
2. ExPASy PeptideCutter
3. ExPASy ProtParam
| None |