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Helical Mimetics secondary structures

This volume brings together most of these critical issues by highlighting recent advances in a number of core areas of peptidomimetic synthesis. Section 9 focuses on side-chain-modified peptides, Section 10 describes the preparation and use of a variety of peptide main-chain modifications. Combined side-chain- and main-chain-modified peptides are covered in Section 11. Finally, Section 12 provides chemistry leading to peptides incorporating secondary structure ((1- and y-turns, helices, p-sheets) mimetics and inducers. [Pg.2]

Complexes that feature a-helices at interfaces were studied because a-helices constitute the largest class of protein secondary structure and mediate many protein interactions [30, 51]. Helices located within the protein core are vital for the overall stability of protein tertiary structure, whereas exposed a-helices on protein surfaces constitute central bioactive regions for the recognition of numerous proteins, DNAs, and RNAs. Importantly, helix mimetics have emerged as a highly effective class of PPI inhibitors [32, 36, 44, 52-55]. [Pg.199]


See other pages where Helical Mimetics secondary structures is mentioned: [Pg.96]    [Pg.369]    [Pg.29]    [Pg.316]    [Pg.190]    [Pg.251]    [Pg.263]    [Pg.486]    [Pg.218]    [Pg.393]    [Pg.92]    [Pg.395]    [Pg.582]    [Pg.36]    [Pg.36]    [Pg.184]   


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Helical Mimetics

Helical structure

Helical structure helicate

Mimetic

Mimetics

Secondary structure

Structural mimetics

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