Date of Award
6-1984
Document Type
Open Access
Degree Name
Bachelor of Science
Department
Chemistry
Language
English
Abstract
The antibiotic action of the ionophore valinomycin is a result of its ability to preferentially bind potassium ions and transport them across cellular membranes. Complexation is solely due to the molecular structure of this cyclic depsipeptide. In solution, the molecule exists in different conformers depending upon solvent polarity. Exact knowledge as to the structure of valinomycin in the aqueous and lipid cellular layers is thus difficult to determine. Many spectral studies of valinomycin have been undertaken utilizing a variety of instrumental methods and conformations existing in different solvents have been proposed. We have performed energy minimization procedures on these structures. Conformations were generated both with and without � symmetry condition. Utilization of these mathematical models resulted in structures which agree with those described in the literature. Thus, these calculations may be combined with solution studies to determine the exact structure of valinomycin before, during and after ion transport.
Recommended Citation
Cohen, Rachel J., "Conformational Energy Calculations on Valinomycin" (1984). Honors Theses. 1895.
https://digitalworks.union.edu/theses/1895
Rights Statement
