Study of the three-dimensional structure of tryptophan zipper peptides through ¹H NMR chemical shifts calculations

Three-dimensional structures of proteins are intimately linked to their functions, therefore understanding their conformation in solution is essential. While nuclear magnetic resonance spectroscopy and X-ray crystallography are widely employed for protein structural determination, their limitations make the process challenging and expensive. Theoretical calculations of chemical shifts present a potential complement to experimental techniques, facilitating the study of protein structures. This investigation aims to assess the applicability of chemical shift calculations in analyzing three-dimensional structures of peptides, focusing on the tryptophan zipper 1 peptide as a model. Furthermore, a mutated variant of this peptide was proposed to evaluate the stability of its structural elements under sequence modifications. Through calculations, a potential structural alteration in the β-turn region of the mutant peptide compared to tryptophan zipper 1 was identified. This research demonstrates the potential of using computational approaches to complement experimental methods in studying protein structures and their functional implications. (author)