
Engineering of stable folded and functional biomolecules has attracted a great deal of research attention recently. Within this field, these researchers are particularly interested in the design, synthesis, and characterization of protein core modules and cyclic Peptide Nucleic Acids (PNAs).
In globular proteins, core motifs can be identified and their elements can be combined in suitable peptides to construct native like modules. The designed peptides consist of core elements from Bovine Pancreatic Trypsin Inhibitor (BPTI) and/or GB1 (a B1 immuno-globulin binding domain) linked by natural or designed sequences, and they contain a strategically placed crosslink to limit conformational space to more collapsed conformations. The ongoing and proposed studies exemplify new approaches and are leading to significant and generalized insights that contribute to the protein folding problem.
Cyclic PNAs are promising candidates to generate nanotubular structures. Such nanotubular reagents can be useful as new catalysts, wire conductors, or drug transport systems. Cyclic PNAs are being designed by means of molecular modeling studies that assess the viability of cyclization as well as the molecular recognition mechanism between cyclic units.
Yvonne Angell, Research Associate
Natalia Carulla, Graduate Student Researcher
Christopher Gross, Graduate Student Researcher
Marta Planas, Facultat de Ciencies, Universitat de Girona, Girona, Spain
Design and characterization studies in this field are computationally intensive. Fortunately, plenty of useful software is available. Once the designed molecules are synthesized, they are the subject of nuclear magnetic resonance (NMR) spectroscopic studies, from which structural features can be calculated.
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