Detailed description of 5054 ID
Primary information
AHTPDB ID5054
PMID5054_link
YEAR2013
SEQUENCEGAAELPCSADWW
LENGTH12
MOL WT1305.43
IC50ND 
pIC50ND
SOURCEBullfrog muscle protein hydrolysate
TESTED ONSHR
PURIFICATIONND
ASSAYND
BITTERNESSND
ISOELECTRIC POINT3.67
SYSTOLIC BP DECREASE10.0 
Secondary information
PropertiesPhysico-Chemical details
STRUCTURE
Structure
DSSP statesCCSSSSSCCCCC
SMILESNCC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@@H]1C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1c[nH]c(C)c1CC)C(=O)N[C@@H](Cc1c[nH]c(C)c1CC)C(=O)O
External Links to PDB, Swiss-Prot and IEDB
PDB exactPDB partialSP exactSP partialIEDB exactIEDB partial
NA NA NA NA
from

TO
NA NA
Reference Informaiton
ARTICLE/REFERENCEIs the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?
AUTHORS/PRIMARY REFERENCEJian-Hui Wang et al.,
JOURNAL/EXTRA LINKSJournal of Molecular Structure 1040 (2013) 164-170