PPIRE00836
Target Protein Information
| Protein_Name | Troponin C, slow skeletal and cardiac muscles |
|---|---|
| Protein_Sequence | MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE |
| Organism_Source | Oryctolagus cuniculus |
| Functional_Classification | EF-hand calcium-binding proteins |
| Cellular_Localization | Cytoplasm |
| Gene_Names | TNNC1 |
| UniProt_ID | P02591 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Ac(Asn-103 |
|---|---|
| Peptide_Sequence | NRDADGYIDAEEL |
| Peptide_Length | 13 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)CNC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)CC(N)=O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Acetyl |
| C-terminal_Modification | amide |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 1480.51 |
|---|---|
| Aliphatic_Index | 75.38462 |
| Aromaticity | 0.07692 |
| Average_Rotatable_Bonds | 3.76923 |
| Charge_at_pH_7 | -3.99798 |
| Isoelectric_Point | 3.60605 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 22 |
| Number_of_Hydrogen_Bond_Donors | 24 |
| Topological_Polar_Surface_Area | 724.24000 |
| X_logP_energy | -7.78003 |
Interaction Information
| Affinity | KD=18.87 uM |
|---|---|
| Affinity_Assay | 1H NMR spectroscopy |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | 1H-NMR studies of synthetic peptide analogues of calcium-binding site III of rabbit skeletal troponin C: effect on the lanthanum affinity of the interchange of aspartic acid and asparagine residues at the metal ion coordinating positions. |
| Release_Year | 1988 |
| PMID | 3415981 |
| DOI | 10.1021/bi00411a043 |