Title of project

Structural Conformation of Octapeptide [Sar1]angiotensin II Using NMR

Faculty Advisor

Dr. John Dwyer

Department

Chemistry

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Structural Conformation of Octapeptide [Sar1]angiotensin II Using NMR

Protein structure is key to proper functioning in biological systems. The biological activities of some proteins are related to their conformation both in solution and in their receptor sites. For this reason, chemists commonly investigate the conformation of such molecules in solution. Angiotensin is a vasoactive octapeptide capable of inducing the contraction of blood vessels. Studies have shown that this octapeptide plays a significant role in maintaining normal blood pressure. In this project, the conformation of [Sar1]angiotensinII (Sar-Arg-Val-Tyr-Ile-His-Pro-Phe) in solution was investigated by proton Nuclear Magnetic Resonance spectroscopy (NMR). Both one dimensional and two dimensional NMR data were used to determine the structure and solution phase conformation of the peptide.