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Efforts Toward Fundamental Studies of Peptide Structures

出版	ProQuest LLC, 2022
URL	http://books.google.com.hk/books?id=6xeC0AEACAAJ&hl=&source=gbs_api

註釋Understanding protein structures at the molecular level is key to establishing protein structure-function relationships and can provide new knowledge to guide protein rational design and to expand the range of protein functions. Specifically, we focus on designing small peptides and peptidomimetics that serve as models for more complicated biological systems. This dissertation describes the use of various biophysical tools, including nuclear magnetic resonance (NMR), liquid chromatography (LC), native mass spectrometry (MS), and X-ray crystallography, to elucidate peptide structures. The first chapter summarizes basic peptide structural elucidation strategies by NMR. The second chapter describes the design of peptide systems that enable the comparisons of Îø-hairpin propensity among peptides with homochiral or heterochiral strands. In this study, Îø-hairpin folding was observed for homochiral peptides with aligned nonpolar side chains, but no Îø-hairpin population was detected for diastereomers in which one strand contains L-residues and the other contains D-residues. The third chapter details our efforts toward backbone thioester exchange systems to study the interactions between D-peptide helices and L-peptide helices. The final chapter describes the design of a heterotrimer system inspired by a stable trimeric foldon scaffold, which would allow induced assembly of diverse protein appendages. In this study, we identified multiple sequence variations of the foldon scaffold that influences trimer formation. Interestingly, we discovered a specific pair of variants that forms a stable aab heterotrimer with a minimal number of mutations. Such findings enhance our understanding of heterotrimer formation and can motivate the rational design of other heterooligomeric structures.