10/25/2022 0 Comments Stapled helix![]() Furthermore, CEEOL allows publishers to reach new audiences and promote the scientific achievements of the Eastern European scientific community to a broader readership. CEEOL offers various services to subscribing institutions and their patrons to make access to its content as easy as possible. The -helix peptide library, with two cysteine residues on the opposite side of the randomized face, was modified with a rigid hydrocarbon staple linker on a phage. Currently, CEEOL covers more than 2000 journals and 690.000 articles, over 4500 ebooks and 6000 grey literature document. A stapled -helix peptide library was designed and constructed using a chemically modified phage display system for screening stapled-peptide ligands against target proteins. CEEOL provides scholars, researchers and students with access to a wide range of academic content in a constantly growing, dynamic repository. Here we describe the discovery and optimization of a stapled helix peptide that binds to the N-terminal domain of the 70 kDa subunit of replication protein A (RPA70N). ![]() Currently, over 1000 publishers entrust CEEOL with their high-quality journals and e-books. Stapled helix peptides can serve as useful tools for inhibiting protein-protein interactions but can be difficult to optimize for affinity. In the rapidly changing digital sphere CEEOL is a reliable source of adjusting expertise trusted by scholars, publishers and librarians. Stapled helix registration#Registration links and more information can be found at is a leading provider of academic e-journals and e-books in the Humanities and Social Sciences from and about Central and Eastern Europe. Among the three macrocyclic crosslinks designed for this purpose, the 15-membered macrocycle, formed by a hept-4. Join one of the industry workshops and visit Booth 701 in the exhibit hall. To improve the helix-stabilizing capability of the stapled N-capping box system, we examined a modified RCM-based crosslinking system with the intention of expanding the hydrophobic microenvironment near the N-terminus of the helix.
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