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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
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
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
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.
Molecular Basis Of The Role Of Kindlin 2 In Cell Adhesion, Hettiarachchige Dhanuja Deepamalee Perera
Molecular Basis Of The Role Of Kindlin 2 In Cell Adhesion, Hettiarachchige Dhanuja Deepamalee Perera
ETD Archive
Kindlins are a novel family of cytoskeleton proteins that plays an important role in the activation of heterodimeric integrin transmembrane receptors. These receptors play a vital role in cell adhesion, cell migration and other cellular processes. The Kindlin protein family consists of three homologous proteins, Kindlin 1, 2 and 3 with differential tissue distribution and varying expression levels in human. Mutations of Kindlin 1 protein are clinically linked to Kindler Syndrome. Kindlin 2 knockdown studies have shown embryonic lethality in mouse, but no diseases have been clinically testified. Kindlin 3 mutations are associated with bleeding disorders, e.g. LADIII. Talin is …
Discovery And Identification Of New Dna Photoproducts And Investigation Of The Redox Mechanism Of Human Apurinic/Apyrimidinic Endonuclease 1 (Hape1) Protein, Dian Su
All Theses and Dissertations (ETDs)
Exposure of cells to ultraviolet light results in the formation of DNA photoproducts, many of which have been linked to skin cancer. The majority of these photoproducts arise from a photoreaction between two pyrimidines. Irradiation of double stranded B form DNA under physiological conditions mainly produces adjacent dimers. Nonadjacent photodimers of both intrastrand and interstrand types are much rarer. Intrastrand-type nonadjacent dimers form when one or more nucleotides between two pyrimidines become extrahelical owing to the formation of single strand DNA or a slipped structure. This allows the two pyrimidines to photodimerize in a colinear arrangement, as if the intervening …