L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine forms an extended peptide chain with diverse hydrophobic, polar, and basic residues. Its sequence length supports complex folding and multivalent binding analysis. The varied side-chain chemistry provides a rich model for studying intramolecular stabilization. Applications include protein-fragment modeling, structural biophysics, and advanced peptide engineering.
CAT No: R2212
CAS No:309246-19-3
Synonyms/Alias:L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine;309246-19-3;L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine;b-Endorphin (rat);beta-Endorphin, rat;??-Endorphin (rat);MFCD00133129;AKOS040754639;DA-79186;G91313;
L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine is a synthetic peptide composed of a complex sequence of amino acids, designed for advanced research applications in biochemical and molecular biology studies. With its intricate arrangement, this compound offers a unique structural framework that can be leveraged to investigate protein-protein interactions, signaling pathways, and conformational dynamics in various experimental settings. Its stable peptide bonds and diverse side chains contribute to its versatility, making it a valuable tool for laboratories focused on unraveling the intricacies of peptide behavior and function. The sequence's combination of polar, nonpolar, and charged residues enables it to participate in a wide range of binding events and structural analyses, supporting its use in both in vitro and in vivo research environments where peptide-based models are essential.
Peptide Structure-Function Studies: L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine serves as an ideal model for dissecting the relationship between peptide sequence and biological function. Researchers utilize this compound to systematically substitute or modify specific residues, allowing for the elucidation of structure-activity relationships that govern peptide stability, folding, and interaction with target molecules. By analyzing the impact of each amino acid within the sequence, insights are gained into the molecular determinants of binding specificity and functional efficacy, thereby advancing the understanding of peptide engineering principles.
Protein Interaction Mapping: In the context of mapping protein-protein interactions, this synthetic peptide offers a controlled and reproducible system for probing the affinity and specificity of binding domains. Its sequence can be immobilized on assay platforms or introduced into cell-free systems to identify interacting partners through pull-down assays, surface plasmon resonance, or co-immunoprecipitation techniques. The resulting data inform the design of peptide inhibitors or mimetics and contribute to the broader effort of delineating complex interaction networks within biological systems.
Enzyme Substrate Analysis: The compound's well-defined primary structure makes it a suitable substrate for enzymatic assays, particularly those investigating protease activity, post-translational modifications, or peptide cleavage specificity. By subjecting this peptide to various enzymes, researchers can monitor reaction kinetics, identify cleavage sites, and characterize enzyme preferences, thereby facilitating the development of new biochemical tools and enhancing the understanding of enzymatic mechanisms at the molecular level.
Biophysical Characterization: L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine is frequently employed in studies utilizing circular dichroism spectroscopy, nuclear magnetic resonance, and X-ray crystallography to investigate secondary and tertiary structure formation. Its sequence complexity allows for the observation of folding patterns, helix-coil transitions, and the influence of environmental factors such as pH, temperature, and solvent conditions on peptide conformation. These analyses are crucial for advancing knowledge in protein folding diseases, peptide therapeutics, and biomaterials design.
Peptide Library Development: As a template for combinatorial peptide library synthesis, this compound provides a foundation for generating diverse analogs with varied biological activities. Researchers can introduce systematic variations at specific positions within the sequence to screen for enhanced binding, stability, or functional properties. The resulting libraries accelerate the discovery of novel peptide leads for further research and support high-throughput screening efforts in drug development, diagnostics, and molecular recognition studies.
In summary, L-tyrosylglycylglycyl-L-phenylalanyl-L-methionyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-lysyl-L-seryl-L-glutaminyl-L-threonyl-L-prolyl-L-leucyl-L-valyl-L-threonyl-L-leucyl-L-phenylalanyl-L-lysyl-L-asparaginyl-L-alanyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-asparaginyl-L-valyl-L-histidyl-L-lysyl-L-lysylglycyl-L-glutamine stands out as a versatile research reagent with broad applicability in peptide structure-function studies, protein interaction mapping, enzyme substrate analysis, biophysical characterization, and peptide library development. Its multifaceted sequence and robust chemical properties enable scientists to explore fundamental questions in molecular biology, biochemistry, and peptide engineering, thereby supporting innovation and discovery across a spectrum of scientific disciplines.
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