‹ ›
MYP_015381
← PREVIOUS NEXT → BACK
Basic Information
2K4L
Antimicrobial
Standard
13 amino acids
C81H147N17O14
Standard
Sequence
IILLLLKKFLKKL
Physicochemical Analysis
1583.14 Da
10.48
3.76
3.55
0.2889
1.46
0.60
0.33
4.45
240.00
0.0769
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
516.60
3.34
18.0
18.0
59.0
112.0
1.0
12.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0029516 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (84.62%) to Temporin-1CEc analog 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. cloacae
6.25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0041674 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (84.62%) to Temporin-1CEc analog 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
S. lactis
1.56 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0046901 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (84.62%) to Temporin-1CEc analog 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Pseudomonas aeruginosa
3.13 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0069509 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (84.62%) to Temporin-1CEc analog 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
B. cereus
6.25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0166750 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (84.62%) to Temporin-1CEc analog 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Escherichia coli
1.56 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
1 2 NEXT LAST
Showing 5 records on this page · Page 1 of 2