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NMR structural studies of functional channel peptides.
Connect to full text Available online
View online- Format:
- Book
- Thesis/Dissertation
- Author/Creator:
- Gesell, Jennifer Joanne.
- Language:
- English
- Subjects (All):
- Biochemistry.
- 0487.
- Penn dissertations--Chemistry.
- Chemistry--Penn dissertations.
- Local Subjects:
- Penn dissertations--Chemistry.
- Chemistry--Penn dissertations.
- 0487.
- Physical Description:
- 138 pages
- Contained In:
- Dissertation Abstracts International 58-11B.
- System Details:
- Mode of access: World Wide Web.
- text file
- Summary:
- Membrane peptides corresponding to the sequences of magainin2, and membrane spanning segment 2 (M2) of the acetylcholine (Ach) receptor and the N-methyl-D-aspartate (NMDA) receptor were biologically expressed and uniformly labeled for solution NMR and solid-state NMR structural studies. The M2 peptides taken from larger receptor proteins were shown to be functional. Solution NMR structures were determined in detergent micelles for all of the peptides. The peptides were also studied in oriented planar lipid bilayers. The orientation with respect to the lipid bilayer was obtained for NMDA M2 while a partial backbone structure was determined for the Ach receptor M2. The results are discussed in the context of recently proposed structural models.
- Notes:
- Thesis (Ph.D. in Chemistry) -- University of Pennsylvania, 1997.
- Source: Dissertation Abstracts International, Volume: 58-11, Section: B, page: 5938.
- Supervisor: Stanley J. Opella.
- Local Notes:
- School code: 0175.
- ISBN:
- 9780591659306
- Access Restriction:
- Restricted for use by site license.
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