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Study of dibenzofuran-based amino acid nucleated antiparallel Beta-sheet using 1D- and 2D- nuclear magnetic resonance spectroscopy
|dc.creator||Espina, Jose Roberto||en_US|
|dc.description||Due to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to firstname.lastname@example.org, referencing the URI of the item.||en_US|
|dc.description||Includes bibliographical references.||en_US|
|dc.description.abstract||Simple amides containing the conforrnationally restricted unnatural amino acid 4-(2-aminoethyl)-6-dibenzofuranpropanoic acid (1) were studied by NMR and FT-IR to ascertain the hydrogen bonding capabilities of 1. The preferred structure in non-competitive solvents is a 15-membered ring hydrogen bonded conformation. Water soluble peptides containing 1 were studied using I D-and 2D-NMR techniques to determine the capability of 1 to nucleate 0-sheet structure formation. The sequence specific assigrunents of the peptides as well as the determination of the secondary structure was accomplished. In solution, at pH-5, both peptides exhibit a welldefined 0-tum structure with the dibenzofuran ring of 1 perpendicular to the plane of the strands, interacting with the hydrophobic side chains of the residues flanking it through a hydrophobic interaction, thus forming a well-defined 0-tum mimetic. This hydrophobic cluster also promotes the formation of the 15-membered ring hydrogen bonded conformation necessary for 0-sheet nucleation.||en_US|
|dc.publisher||Texas A&M University||en_US|
|dc.rights||This thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.||en_US|
|dc.title||Study of dibenzofuran-based amino acid nucleated antiparallel Beta-sheet using 1D- and 2D- nuclear magnetic resonance spectroscopy||en_US|
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