H-Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Gly-OH combines basic, acidic, and hydrophobic residues to support studies of extended peptide folding. Its sequence enables mapping of helix-coil transitions. Researchers evaluate conformational ensembles to identify active submotifs. The molecule aids receptor-binding and structural modeling.
CAT No: P6619
CAS No:81156-93-6
Synonyms/Alias:RR-Src;Arg-arg-leu-ile-glu-asp-ala-glu-tyr-ala-ala-arg-gly;81156-93-6;Arginyl-arginyl-leucyl-isoleucyl-glutamyl-aspartyl-alanyl-glutamyl-tyrosyl-alanyl-alanyl-arginyl-glycine;Src-Peptide;Glycine, L-arginyl-L-arginyl-L-leucyl-L-isoleucyl-L-alpha-glutamyl-L-alpha-aspartyl-L-alanyl-L-alpha-glutamyl-L-tyrosyl-L-alanyl-L-alanyl-L-arginyl-;CHEMBL412066;SCHEMBL5665088;HY-P0200;AKOS024456423;FR73585;PD079001;CS-0021294;fluoro[hydroxy(phenyl)phosphoryl]methyl(phenyl)phosphinic acid;
1. TMEM16F and dynamins control expansive plasma membrane reservoirs
2. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
3. Myotropic activity of allatostatins in tenebrionid beetles
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