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

Bibliographic Details
Main Author: Espina, Jose Roberto, 1966-
Format: Thesis eBook
Language:English
Published: [Place of publication not identified] : [publisher not identified] ; 1994.
Subjects:
Online Access:Link to OAKTrust copy
Description
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
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.