Franklin

NMR structural studies of functional channel peptides [electronic resource].

Author/Creator:
Gesell, Jennifer Joanne.
Format/Description:
Book
138 p.
Contained In:
Dissertation Abstracts International 58-11B.

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Details

Subjects:
Biochemistry.
Local subjects:
Penn dissertations -- Chemistry. (search)
Chemistry -- Penn dissertations. (search)
System Details:
Mode of access: World Wide Web.
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.
Contributor:
Opella, Stanley J., advisor
University of Pennsylvania.
ISBN:
9780591659306
Access Restriction:
Restricted for use by site license.