Protein-mimetic Structures

Proteins derive their powerful and diverse capacity for molecular recognition and catalysis from their ability to fold into defined secondary and tertiary structures and display specific functional groups at precise locations in space. Functional protein domains are typically 50-200 residues in length and utilize a specific sequence of side chains to encode folded structures that have a compact hydrophobic core and a hydrophilic surface. Mimicry of protein structure and function by non-natural ohgomers such as peptoids wiU not only require the synthesis of 50mers with a variety of side chains, but wiU also require these non-natural sequences to adopt, in water, tertiary structures that are rich in secondary structure. 

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Section 13.1 concludes with a consideration of some additional protein mimetic structures (Section 13.1.3). This part deals primarily with the development of a molecular tool kit that can lead to locked-in folds, bundles, and other molecular arrays (Section 13.1.3.1). An application leading to zinc finger mimetics is also presented (Section 13.1.3.1.2) J6 ... 

Since serine shows a high occurrence at the exposed positions (i+1) and (i+2) of P-tums in protein crystal structures,138,185 it was decided to investigate whether or not the (/ )- and (S)- a-chimeras of Asp-Ser would be interesting P-turn mimetics at the (i+Imposition of P-turns. Furthermore, it was of interest to see whether or... 

Chemogenomics with Protein Secondary-Structure Mimetics... 

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]. 

Protein Secondary Structure Mimetics as Modulators of Protein-Protein and Protein-Ligand Interactions... 

In 1980, Farmer, with great foresight, proposed the use of cyclohexane as a scaffold to project functionality as a mimetic of protein secondary structures... 

Electrochemical impedance spectroscopy provides a sensitive means for characterizing the structure and electrical properties of the surface-bound membranes. The results from impedance analysis are consistent with a single biomembrane-mimetic structure being assembled on metal and semiconductor electrode surfaces. The structures formed by detergent dialysis may consist of a hydrophobic alkyl layer as one leaflet of a bilayer and the lipid deposited by dialysis as the other. Proteins surrounded by a bound lipid layer may simultaneously incorporate into pores in the alkylsilane layer by hydrophobic interactions during deposition of the lipid layer. This model is further supported by the composition of the surface-bound membranes and by Fourier transform infrared analyses (9). 

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