Abstract
Small molecules which can mimic the key structural facets of protein secondary structure, in particular the α-helix, β-strand, and β-sheet, have been shown to be potent disruptors of protein-protein interactions. Researchers have recently taken the organizational imitation of protein secondary structure to a new level by using intramolecular hydrogen bonds as stabilizing forces in these small molecule mimetics. The inclusion of these interactions invokes a conformational bias of the system, allowing for greater control of the appearance, and thus often function, of these molecules by design.
Original language | English (US) |
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Pages (from-to) | 1-23 |
Number of pages | 23 |
Journal | Current Topics in Microbiology and Immunology |
Volume | 348 |
DOIs | |
State | Published - 2011 |
ASJC Scopus subject areas
- Immunology and Allergy
- Microbiology (medical)
- Immunology
- Microbiology