Presentation Title

Modeling the Effects of Microgravity On Oxidation in Mitochondria: A Protein Damage Assessment Across a Diverse Set of Life Forms

Advisor Information

Dhundy Bastola

Location

UNO Criss Library, Room 112

Presentation Type

Oral Presentation

Start Date

7-3-2014 9:15 AM

End Date

7-3-2014 9:30 AM

Abstract

The exposure to stress at the microbiological level may likely cause life-sustaining proteins and tissues to fail. The effects of microgravity from space flights(weightlessness) and muscular disuse (as in the case of bed-rest) are thought to impose hardships on muscular proteins, which can result into atrophy. After an exposure to microgravity, astronauts may lose much muscle strength and mass.Carbonyl derivatives are the result of direct metal-catalysed oxidation that interacts with the carbonylatable amino-acid side chains of arginine (R), lysine (K), threonine (T) and proline (P) residues. Incited by stress, sites containing these amino-acids may attract oxidation and degradation in protein. Mitochondria are small organelles that are responsible for many extremely important “house-keeping” functions related to cellular health. Mitochondria primarily produce the energy for the eukaryote cells using oxidative processes. Since the consequences of oxidative reactions on protein are often dangerous, we hypothesize that these reactions are highly contained in mitochondria to minimize local oxidative damage. In this study, we present the composition of oxidative sites across mitochondrial and non-mitochondria (enzymatic and non-enzymatic) proteins from a diverse group of organisms. Our major finding is that mitochondrial proteins contain far fewer oxidative sites than the non-mitochondrial variety. We maintain that sites may have been naturally removed in life-sustaining proteins for evolutionary purposes. This study helps to explain protein tolerances to oxidation based on the composition of these sites.

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Mar 7th, 9:15 AM Mar 7th, 9:30 AM

Modeling the Effects of Microgravity On Oxidation in Mitochondria: A Protein Damage Assessment Across a Diverse Set of Life Forms

UNO Criss Library, Room 112

The exposure to stress at the microbiological level may likely cause life-sustaining proteins and tissues to fail. The effects of microgravity from space flights(weightlessness) and muscular disuse (as in the case of bed-rest) are thought to impose hardships on muscular proteins, which can result into atrophy. After an exposure to microgravity, astronauts may lose much muscle strength and mass.Carbonyl derivatives are the result of direct metal-catalysed oxidation that interacts with the carbonylatable amino-acid side chains of arginine (R), lysine (K), threonine (T) and proline (P) residues. Incited by stress, sites containing these amino-acids may attract oxidation and degradation in protein. Mitochondria are small organelles that are responsible for many extremely important “house-keeping” functions related to cellular health. Mitochondria primarily produce the energy for the eukaryote cells using oxidative processes. Since the consequences of oxidative reactions on protein are often dangerous, we hypothesize that these reactions are highly contained in mitochondria to minimize local oxidative damage. In this study, we present the composition of oxidative sites across mitochondrial and non-mitochondria (enzymatic and non-enzymatic) proteins from a diverse group of organisms. Our major finding is that mitochondrial proteins contain far fewer oxidative sites than the non-mitochondrial variety. We maintain that sites may have been naturally removed in life-sustaining proteins for evolutionary purposes. This study helps to explain protein tolerances to oxidation based on the composition of these sites.