Study of dibenzofuran-based amino acid nucleated antiparallel Beta-sheet using 1D- and 2D- nuclear magnetic resonance spectroscopy /
a welldefined 0-tum structure with the dibenzofuran ring of 1
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1994.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | a welldefined 0-tum structure with the dibenzofuran ring of 1 accomplished. In solution, at pH - 5, both peptides exhibit acid (1) were studied by NMR and FT-IR to ascertain the bonded conformation necessary for 0-sheet nucleation. bonded conformation. Water soluble peptides containing 1 defined 0-tum mimetic. This hydrophobic cluster also hydrogen bonding capabilities of 1. The preferred structure in non-competitive solvents is a 15-membered ring hydrogen perpendicular to the plane of the strands, interacting with promotes the formation of the 15-membered ring hydrogen Simple amides containing the conforrnationally restricted the capability of 1 to nucleate 0-sheet structure formation. the determination of the secondary structure was the hydrophobic side chains of the residues flanking it The sequence specific assigrunents of the peptides as well as through a hydrophobic interaction, thus forming a well- unnatural amino acid 4-(2-aminoethyl)-6-dibenzofuranpropanoic were studied using I D- and 2D-NMR techniques to determine |
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| Item Description: | "Major subject: Chemistry". In title, numerals and symbol for Greek letter Beta are used. Vita. |
| Physical Description: | x, 62 leaves : illustrations ; 28 cm. Also available online. |
| Bibliography: | Includes bibliographical references. |