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Full-Text Articles in Physical Sciences and Mathematics

10th Annual Senior Research Symposium Of The Department Of Biological Sciences, Chemistry And Biochemistry, Messiah College Dec 2010

10th Annual Senior Research Symposium Of The Department Of Biological Sciences, Chemistry And Biochemistry, Messiah College

School of Science, Engineering & Health (SEH) Symposium

No abstract provided.


Circular Dichroism Spectroscopy In The Undergraduate Curriculum, Adam R. Urbach Sep 2010

Circular Dichroism Spectroscopy In The Undergraduate Curriculum, Adam R. Urbach

Chemistry Faculty Research

Circular dichroism spectropolarimetry (CD) is a method of optical spectroscopy that seems in most practical ways like UV−visible spectroscopy. The main difference between the two methods is that CD, instead of measuring the absorbance of light as a function of wavelength, measures the difference in absorbance of left versus right circularly polarized light as a function of wavelength. A CD spectrum is an observation of the structure of a chiral compound; it often serves as a “fingerprint” of the structure of biological molecules such as proteins and nucleic acids. For this reason, CD has been broadly applied in biochemistry and …


Frataxin And Mitochondrial Fes Cluster Biogenesis, Timothy L. Stemmler, Emmanuel Lesuisse, Debumar Pain, Andrew Dancis Aug 2010

Frataxin And Mitochondrial Fes Cluster Biogenesis, Timothy L. Stemmler, Emmanuel Lesuisse, Debumar Pain, Andrew Dancis

Biochemistry and Molecular Biology Faculty Publications

Friedreich’s ataxia is an inherited neurodegenerative disease caused by frataxin deficiency. Frataxin is a conserved mitochondrial protein that plays a role in Fe-S cluster assembly in mitochondria. Fe-S clusters are modular cofactors that perform essential functions throughout the cell. They are synthesized by a multi-step and multi-subunit mitochondrial machinery that includes a scaffold protein Isu for assembling a protein bound Fe-S cluster intermediate. Frataxin interacts with Isu, iron, and with the cysteine desulfurase Nfs1 that supplies sulfur, thus placing it at the center of mitochondrial Fe-S cluster biosynthesis.