LEADER 03953cam 2200613 i 4500001 on1332541700 003 OCoLC 005 20240122153503.0 006 m o d 007 cr unu|||||||| 008 220623s2022 ncua obm 000 0 eng d 035 (Sirsi) o1332541700 035 (OCoLC)1332541700 040 ERE |beng |erda |cERE |dOCLCQ |dOCLCF |dOCLCO |dERE |dUtOrBLW 049 EREE 090 QP603.L56 100 1 Roberts, Daniella, |eauthor. |?UNAUTHORIZED 245 10 Biophysical investigation into the protein dynamics governing the allosteric regulation of plant and animal 15-lipoxygenases / |cby Daniella Roberts. 264 1 [Greenville, N.C.] : |b[East Carolina University], |c2022. 300 1 online resource (111 pages) : |billustrations (some color) 336 text |btxt |2rdacontent 337 computer |bc |2rdamedia 338 online resource |bcr |2rdacarrier 347 text file 347 |bPDF 347 |c5.587 MB 538 System requirements: Adobe Reader. 538 Mode of access: World Wide Web. 502 |bM.S. |cEast Carolina University |d2022 500 Presented to the Faculty of the Department of Chemistry 500 Advisor: Adam R. Offenbacher 500 Title from PDF t.p. (viewed December 6, 2023). 520 3 Lipoxygenases (LOXs) are a family of enzymes found in plants, animals, fungi, and bacteria that catalyze the per-oxidation of polyunsaturated fatty acids. In plants, LOXs are involved in growth, development, and defense against pathogenic attacks. There are also multiple isoforms present in humans, which have contradictory roles in the body. Specifically, human 15-LOX isoforms, 15-LOX-1 and 15-LOX-2, are involved in both homeostasis and pro-inflammatory pathways. In order to selectively target the activity of these enzymes, research has turned to allosteric regulation, which is the focus of this Thesis. Previously, the allosteric regulation of a model plant 15-LOX, soybean lipoxygenase-1 (SLO), has been characterized using hydrogen-deuterium exchange mass spectrometry (HDX-MS), revealing that the addition of the allosteric effector, oleyl sulfate (OS), alters a specific region of the enzyme. Herein, we used a combination of thermodynamic and biophysical techniques such as isothermal titration calorimetry and differential scanning calorimetry to investigate the allosteric regulation of SLO by OS. We present data which supports that the allosteric regulation of SLO by OS does not induce oligomerization or large-scale conformational changes and that the allostery is dynamically driven. We also employed HDX-MS to study the dynamics of 15-LOX-1 compared to previously collected data of 15-LOX-2 to reveal structural differences between the two isozymes that may explain their altered catalytic behavior. 504 Includes bibliographical references. 650 0 Lipoxygenases. |=^A1385445 650 0 Enzymes. |=^A458 650 0 Chemical kinetics. |=^A85449 653 Allostery 653 Protein Dynamics 653 Steady-State Kinetics 653 Hydrogen-Deuterium Exchange Mass Spectrometry 655 7 dissertations. |2aat |0(CStmoGRI)aatgf300028029 655 7 Academic theses. |2fast |0(OCoLC)fst01726453 655 7 Academic theses. |2lcgft 655 7 Thèses et écrits académiques. |2rvmgf |0(CaQQLa)RVMGF-000001173 700 1 Offenbacher, Adam R., |edegree supervisor. |?UNAUTHORIZED 710 2 East Carolina University. |bDepartment of Chemistry. |?UNAUTHORIZED 856 40 |uhttp://hdl.handle.net/10342/10684 |zAccess via ScholarShip 949 |owjh 994 C0 |bERE 596 1 4 998 5831726