Difference between revisions of "Part:BBa K2113004"
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<br>Grand average of hydropathicity (GRAVY): -2.043
 
<br>Grand average of hydropathicity (GRAVY): -2.043
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===ExPASy Peptide Cutter Results===
 +
(The following information has been contributed by SVCE_Chennai iGEM-2016)
 +
 +
<table border="1">
 +
<tr>
 +
<th>Name of enzyme</th>
 +
<th>No. of cleavages</th>
 +
<th>Positions of cleavage sites</th>
 +
</tr>
 +
<tr>
 +
<td>Arg-C proteinase</td>
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<td>3</td>
 +
<td>3 5 7</td>
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</tr>
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<tr>
 +
<td>BNPS-Skatole</td>
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<td>3</td>
 +
<td>2 4 6</td>
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</tr>
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<tr>
 +
<td>CNBr</td>
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<td>1</td>
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<td>1</td>
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</tr>
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<tr>
 +
<td>Chymotrypsin-high specificity (C-term to [FYW], not before P)</td>
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<td>3</td>
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<td>2 4 6</td>
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</tr>
 +
<tr>
 +
<td>Chymotrypsin-low specificity (C-term to [FYWML], not before P)</td>
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<td>4</td>
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<td>1 2 4 6</td>
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</tr>
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<tr>
 +
<td>Clostripain</td>
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<td>3</td>
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<td>3 5 7</td>
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</tr>
 +
<tr>
 +
<td>Iodosobenzoic acid</td>
 +
<td>3</td>
 +
<td>2 4 6</td>
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</tr>
 +
<tr>
 +
<td>Pepsin (pH>2)</td>
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<td>4</td>
 +
<td>1 2 4 6</td>
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</tr>
 +
<tr>
 +
<td>Proteinase K</td>
 +
<td>3</td>
 +
<td>2 4 6</td>
 +
</tr>
 +
<tr>
 +
<td>Trypsin</td>
 +
<td>3</td>
 +
<td>3 5 7</td>
 +
</tr>
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</table>

Revision as of 07:24, 14 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.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



Mobyle@RPBS 3D Structure Prediction

(The following information has been contributed by SVCE_Chennai iGEM-2016)



3D Structure

MGG.gif


ProtParam Results

(The following information has been contributed by SVCE_Chennai iGEM-2016)

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 information has been contributed by SVCE_Chennai iGEM-2016)

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