By K. Dane Wittrup, Gregory L. Verdine
This quantity of tools in Enzymology appears at Protein Engineering for Therapeutics. The chapters provide an priceless source for teachers, researchers and scholars alike. With a global board of authors, this quantity is divided into sections that hide topics such as Peptides, and Scaffolds
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Additional info for Protein Engineering for Therapeutics, Part B
LEE VOLUME 243. Inorganic Microbial Sulfur Metabolism Edited by HARRY D. , AND JEAN LEGALL VOLUME 244. Proteolytic Enzymes: Serine and Cysteine Peptidases Edited by ALAN J. BARRETT VOLUME 245. Extracellular Matrix Components Edited by E. RUOSLAHTI AND E. ENGVALL VOLUME 246. Biochemical Spectroscopy Edited by KENNETH SAUER VOLUME 247. Neoglycoconjugates (Part B: Biomedical Applications) Edited by Y. C. LEE AND REIKO T. LEE VOLUME 248. Proteolytic Enzymes: Aspartic and Metallo Peptidases Edited by ALAN J.
As an internal modification must be installed at a position on the stapled peptide that is not involved in the intended interface with the target, it is important to consult high-resolution structural information or the results of amino acid mutagenesis experiments to choose an optimal site for internal modification.
2B). Though SAHM1 is less than one-third the length of the dominant-negative MAML peptide, it inhibited the interaction of the dominant-negative MAML peptide with the NOTCH–CSL binary complex with an IC50 of approximately 4mM. After identifying a stapled peptide that interacts with the target, an important parallel aspect is to design a negative control stapled peptide 12 Gregory L. Verdine and Gerard J. Hilinski that can be used to confirm target-specific effects in vitro and in vivo. The design of a negative control stapled peptide is highly context dependent, and thus it is difficult here to provide a general design proscription.