E70K is a point-modified peptide or protein fragment featuring a glutamate-to-lysine substitution that alters charge distribution and electrostatic interactions. This mutation introduces a basic side chain, reshaping local hydrogen-bond patterns and structural propensity. Researchers use it to evaluate mutation-driven conformational changes and binding specificity. Applications include structure-function mapping, electrostatic surface analysis, and protein-engineering investigations.
CAT No: R2796
E70K is a carbohydrate compound that has garnered significant attention in the field of biochemical research due to its unique structural properties and versatile reactivity. Characterized by a specific amino acid substitution at position 70, where glutamic acid (E) is replaced by lysine (K), E70K is often studied in the context of glycoproteins and enzyme-ligand interactions. The alteration in its molecular structure not only impacts its charge distribution but also modulates its interaction with various biological molecules, making it a valuable tool for scientific investigations. Researchers appreciate E70K for its capacity to model post-translational modifications and mimic disease-related mutations in carbohydrate-binding proteins, thereby advancing the understanding of molecular mechanisms underlying cellular processes.
Protein Engineering: E70K serves as an essential model for exploring the effects of site-specific mutations on protein-carbohydrate interactions. By introducing the E70K mutation into glycoproteins or carbohydrate-recognizing domains, scientists can systematically examine the resulting changes in binding affinities and conformational dynamics. This approach is instrumental in elucidating the role of specific amino acids in substrate recognition and catalysis, thereby aiding the rational design of engineered proteins with tailored properties for use in industrial biotechnology and synthetic biology applications.
Structural Biology: The E70K variant is frequently utilized in structural biology studies to investigate the three-dimensional organization of carbohydrate-binding proteins. Advanced techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy benefit from the predictable alteration in electrostatic surface potential imparted by the E70K substitution. These studies provide insight into the molecular determinants of specificity and affinity in carbohydrate-protein complexes, facilitating the development of computational models that predict the effects of similar mutations in related systems.
Enzyme Mechanism Elucidation: In enzymology, E70K is employed to dissect the catalytic mechanism of carbohydrate-active enzymes. The presence of lysine at position 70 can influence the protonation state and orientation of active site residues, thereby impacting substrate turnover and reaction kinetics. Through kinetic assays and mutagenesis experiments, researchers use E70K to identify key intermediates and transition states, ultimately contributing to a deeper understanding of enzyme function and the development of novel biocatalysts for synthetic applications.
Disease Mutation Modeling: E70K is also leveraged as a model for studying disease-associated mutations in carbohydrate-binding proteins. In genetic disorders where similar amino acid substitutions occur, the E70K mutation can be introduced into homologous proteins to replicate pathogenic phenotypes in vitro. This enables researchers to probe the molecular basis of altered carbohydrate recognition, aggregation, or signaling, providing a foundation for the identification of potential therapeutic targets and the design of small-molecule modulators.
Biophysical Characterization: The E70K carbohydrate compound is extensively characterized using a range of biophysical techniques to assess its stability, folding, and interaction with other biomolecules. Techniques such as circular dichroism spectroscopy, differential scanning calorimetry, and isothermal titration calorimetry offer quantitative insights into the thermodynamic and kinetic parameters governing E70K behavior. These data are invaluable for benchmarking computational models, guiding mutagenesis strategies, and optimizing conditions for downstream analytical or preparative workflows. By integrating E70K into multidisciplinary research programs, scientists can harness its unique properties to drive innovation across protein engineering, structural biology, enzymology, disease modeling, and biophysical analysis, underscoring its broad utility in carbohydrate-related studies.
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