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Messiah College: MOSAIC (Messiah's Open Scholarship And Intellectual Creativity)
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    Blue River, Grey Skies

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    Nature photograp

    Furry Friend

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    Squirrel in winte

    295 South

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    Sunset on the highwa

    Floral Webs

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    Flowers and shrubs covered in spider web

    Table of Contents

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    Table of Contents for the 2023 Peregrine Review Art Photography Poetry Pros

    Effectiveness of Mechanical Versus Manual Traction in Reducing Cervical Radiculopathy Pain and Disability

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    Purpose To compare cervical traction methods and determine the most effective method for treating cervical radiculopathy to reduce pain and disability in patients aged 20-70 years old. Introduction Cervical radiculopathy is a common musculoskeletal disorder resulting in pain and disability among patients seeking physical therapy services. Radicular pain arising from irritation of cervical spine nerve roots affects approximately one in every thousand individuals and the cost associated with diagnosis and treatment for this condition places a substantial burden on the healthcare system. The estimated non-operative cost to an average patient is $1,143 and is often accompanied by up to 10 months lost at work

    2023 SACS Symposium Schedule

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    Thank you for joining us as we celebrate the excellent research that has been conducted by the students of the School of Arts, Culture and Society. The week will kick-off with a research symposium on: Monday, April 24th in Hostetter Chapel from 8 am - 8 pm Student researchers will presenting their data in both poster and oral presentation formats. At Messiah, we believe in educating men and women toward maturity of intellect, character and Christian faith . Through inquiry and scholarship, our students and faculty seek to glorify God and grow in wisdom and understanding of His creation. Dr. Peter Powers, Dean of the School of Arts, Culture and Society Dr. Jennifer Thomson, Symposium Coordinato

    Time Dominoes

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    https://mosaic.messiah.edu/kits/1699/thumbnail.jp

    Catan

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    https://mosaic.messiah.edu/libraryofthings/1058/thumbnail.jp

    An Engineered Artificial Selection System for the Directed Evolution of Unnatural Cytochrome C Biosynthesis Enzymes

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    Cytochrome c (cyt c) is a small, stable electron transfer protein with a covalently ligated heme group that has shown promise as a target for catalyst design. Variation of the transition metal in the heme center of cyt c greatly affects the redox potential of the mature metalloprotein, but chemical substitution procedures are costly and difficult to scale. Nevertheless, artificial non-ferrous hemoproteins catalyze an abundance of interesting abiological transformations, and alternative preparation methods would allow for a broader exploration of their properties. Through laboratory evolution and enzyme activity studies, residues responsible for substrate specificity in heme c biosynthesis enzymes have been identified. The mechanism of holocytochrome c-type synthase (HCCS)—the enzyme that catalyzes the covalent ligation of heme to cyt c—is not fully characterized, so rational engineering of the enzyme to specifically attach non-ferrous transition metal-substituted hemes to apocyt c is difficult. Directed evolution allows for the screening of vast libraries of enzyme mutants in a single experiment, making it feasible to rapidly evolve HCCS variants with substrate specificities tuned for non-ferrous heme cofactors. Using a rational approach based on molecular modeling, a selection vector was designed and cloned to modulate cell growth based on covalent heme-attachment. The selection vector was transformed into E. coli alongside a heme uptake vector and a library of HCCS mutants. After transformants were grown in cycles of positive and negative selection, variants were isolated and sequenced to identify dominant mutations conferring non-ferrous transition metal selectivity to HCCS. Verifying the efficacy of this selection system for the directed evolution of HCCS variants will directly enable the tuning of other enzymes involved in cyt c biogenesis. Furthermore, it could enable the retuning of analogous biosynthesis pathways for other covalent heme proteins, unlocking a matrix of new-to-nature biosynthetic heme c-containing enzymes

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    Messiah College: MOSAIC (Messiah's Open Scholarship And Intellectual Creativity)
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