Examining the Binding Affinity of Ribose to YME1L-AAA+ By Competition Titrations

dc.contributor.authorWest, Justin
dc.date.accessioned2021-08-10T10:18:41Z
dc.date.available2021-08-10T10:18:41Z
dc.date.issued2021-04-21
dc.description.abstractYME1L is an ATP-dependent protease that is involved in both protein quality control and regulation of mitochondrial morphology. One method to detect binding interactions of this protein is through the use of a fluorescently tagged ATP, known as MANT-ATP. ATP is made of a sugar, ribose, a triphosphate group, and a nitrogenous base, adenine. Binding assays that utilize MANT-ATP have been widely used, but sometimes questioned due to possible non-specific binding interactions. The purpose of this study is to look at the difference in interactions between unmodified ATP and the fluorescent analog MANT-ATP. Results show that MANT-ATP binds to not only the active site of the protein, but possibly multiple sites due to non-specific interactions occurring at high MANT-ATP concentration. Furthermore, we look at how ATP binding is affected by the presence of ribose to look at a possible competition effect. These results show that ribose is in fact able to bind to the ATP binding site alone without the presence of adenine or the phosphates.en_US
dc.identifier.urihttps://jewlscholar.mtsu.edu/handle/mtsu/6544
dc.language.isoen_USen_US
dc.publisherUniversity Honors College Middle Tennessee State Universityen_US
dc.subjectCollege of Basic and Applied Sciencesen_US
dc.subjectMitochondriaen_US
dc.subjectYME1Len_US
dc.subjectAAA+en_US
dc.subjectATPen_US
dc.subjectRiboseen_US
dc.subjectMANT-ATPen_US
dc.subjecttitrationen_US
dc.subjectequilibrium constanten_US
dc.subjectcompetitionen_US
dc.subjectspecific interactionen_US
dc.subjectFRETen_US
dc.subjecttryptophanen_US
dc.subjectfluorescenceen_US
dc.titleExamining the Binding Affinity of Ribose to YME1L-AAA+ By Competition Titrationsen_US
dc.typeThesisen_US

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