Difference between revisions of "Part:BBa K2113004"
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It consists of cationic anti-microbial peptides (AMP) with consecutive sequences of arginine and tryptophan (WRWRWR).This can be used as an antimicrobial agent against a wide range of gram positive and gram negative bacteria. | It consists of cationic anti-microbial peptides (AMP) with consecutive sequences of arginine and tryptophan (WRWRWR).This can be used as an antimicrobial agent against a wide range of gram positive and gram negative bacteria. | ||
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− | ===ProtParam Results=== | + | ===ProtParam Results(Physical and Chemical Properties)=== |
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===ExPASy Peptide Cutter Results=== | ===ExPASy Peptide Cutter Results=== | ||
+ | The following enzymes cleave this peptide. | ||
<table border="1"> | <table border="1"> | ||
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<br>Thrombin | <br>Thrombin | ||
<br>Tobacco etch virus protease | <br>Tobacco etch virus protease | ||
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+ | <!-- Add more about the biology of this part here | ||
+ | ===Usage and Biology=== | ||
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+ | <!-- --> | ||
+ | <span class='h3bb'>Sequence and Features</span> | ||
+ | <partinfo>BBa_K2113004 SequenceAndFeatures</partinfo> | ||
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+ | <!-- Uncomment this to enable Functional Parameter display | ||
+ | ===Functional Parameters=== | ||
+ | <partinfo>BBa_K2113004 parameters</partinfo> | ||
+ | <!-- --> | ||
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Latest revision as of 05:07, 17 October 2016
AMP without glycine
It consists of cationic anti-microbial peptides (AMP) with consecutive sequences of arginine and tryptophan (WRWRWR).This can be used as an antimicrobial agent against a wide range of gram positive and gram negative bacteria.
ProtParam Results(Physical and Chemical Properties)
Number of amino acids: 7
Molecular weight: 1176.41
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) 56
Hydrogen (H) 77
Nitrogen (N) 19
Oxygen (O) 8
Sulfur (S) 1
Formula: C56H77N19O8S1
Total number of atoms: 161
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): 14.026
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 172.23
This classifies the protein as unstable.
Aliphatic index: 0.00
Grand average of hydropathicity (GRAVY): -2.043
ExPASy Peptide Cutter Results
The following enzymes cleave this peptide.
Name of enzyme | No. of cleavages | Positions of cleavage sites |
---|---|---|
Arg-C proteinase | 3 | 3 5 7 |
BNPS-Skatole | 3 | 2 4 6 |
CNBr | 1 | 1 |
Chymotrypsin-high specificity (C-term to [FYW], not before P) | 3 | 2 4 6 |
Chymotrypsin-low specificity (C-term to [FYWML], not before P) | 4 | 1 2 4 6 |
Clostripain | 3 | 3 5 7 |
Iodosobenzoic acid | 3 | 2 4 6 |
Pepsin (pH>2) | 4 | 1 2 4 6 |
Proteinase K | 3 | 2 4 6 |
Trypsin | 3 | 3 5 7 |
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
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]
References
2. ExPASy PeptideCutter
3. ExPASy ProtParam