Presentation Title

Fluorescence Studies of Lysyl Oxidase

Start Date

November 2016

End Date

November 2016

Location

HUB 302-28

Type of Presentation

Poster

Abstract

Lysyl oxidase, an extracellular enzyme, is responsible for catalyzing the formation of crosslinks between elastin and collagen. Its mechanism is a key contributor in the stability and proper development of organisms, especially for skin and connective tissues in humans. Much research has been done in recent years to discover more about its physical characteristics. One way of analyzing the structure of proteins is through fluorescence spectrophotometry; the emission of light by each protein sample is indicative of its relative degree of exposure to water. An excitation-emission matrix (EEM) has been produced for each of the following variations of LOX: pLOX09 (with solubility tag Nus-A), as well as pLOX20 (H303D mutant) and pLOX21 (H303E mutant). The preliminary results show excitation-emission maxima of (341 nm, 282 nm) for pLOX09, (339 nm, 280 nm) for pLOX20, and (340 nm, 284 nm) for pLOX21. The untagged, wild-type lysyl oxidase is currently being tested in order to establish a baseline for comparison with the EEM’s recorded thus far. When compared to this wild-type, it is suggested that larger emission wavelengths (relatively less energetic emissions) indicate a protein that is more exposed to water/less tightly packed. These data can be used to piece together the structural influences of different mutations/variations of lysyl oxidase.

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Nov 12th, 1:00 PM Nov 12th, 2:00 PM

Fluorescence Studies of Lysyl Oxidase

HUB 302-28

Lysyl oxidase, an extracellular enzyme, is responsible for catalyzing the formation of crosslinks between elastin and collagen. Its mechanism is a key contributor in the stability and proper development of organisms, especially for skin and connective tissues in humans. Much research has been done in recent years to discover more about its physical characteristics. One way of analyzing the structure of proteins is through fluorescence spectrophotometry; the emission of light by each protein sample is indicative of its relative degree of exposure to water. An excitation-emission matrix (EEM) has been produced for each of the following variations of LOX: pLOX09 (with solubility tag Nus-A), as well as pLOX20 (H303D mutant) and pLOX21 (H303E mutant). The preliminary results show excitation-emission maxima of (341 nm, 282 nm) for pLOX09, (339 nm, 280 nm) for pLOX20, and (340 nm, 284 nm) for pLOX21. The untagged, wild-type lysyl oxidase is currently being tested in order to establish a baseline for comparison with the EEM’s recorded thus far. When compared to this wild-type, it is suggested that larger emission wavelengths (relatively less energetic emissions) indicate a protein that is more exposed to water/less tightly packed. These data can be used to piece together the structural influences of different mutations/variations of lysyl oxidase.