Membrane protein structure is continuing to be a topic of interest in the scientific community. However, high resolution structural data of these proteins is difficult to obtain. In this study we attempt to use Nuclear Magnetic Resonance (NMR) to begin investigating the finer structural aspects of membrane protein OEP16. Latest structural information suggest a multimer consisting strongly of alpha helices. The amino acid transporter located on the outer membrane of chloroplast organelles, Outer Envelope Protein 16kDa (OPE16) was expressed recombinantly in E. coli BL21 (DE3) cells for use in NMR spectroscopy. Uniform isotopic labeling with 13C and 15N together with 80% perdeuteration allowed for ∼90% of the polypeptide/protein backbone assignments to be carried out using the three dimensional experiments HNCO, HN(CA) CO, HNCA, HN(CO)CA, HNCACB, and CBCA(CO)NH using a 600 MHz spectrometer equipped with a cryoprobe. Chemical shift indices were analyzed for secondary structure through TALOS and PECAN algorithms. Together with NOE connectivities these will enable bond-angle restraints to be introduced for calculating a structural model of the protein. In addition we expressed OEP16 with 15N uniform isotope labeling for relaxation measurements of protein structural dynamics. In order to separate the flexible regions from the rigid regions of the protein, TOCSY-HSQC, HSQC-TOCSY, and NOESY-HSQC experiments were performed on 15N-OEP16 to aid in the assignment of side chains and obtain spatial restraints for use in the determination of three dimensional structure. Results of NMR analysis are compared to results of characterizing the protein by dynamic light scattering (DLS) and circular dichroism (CD) spectroscopy. The findings described in this study provide the first steps in the structure determination of OEP16 and will ultimately contribute to the now limited library of membrane protein structures.