Matching Items (655)
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- All Subjects: Songs (High voice) with piano
ContributorsWasbotten, Leia (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-30
Description
Libby Larsen is one of the most performed and acclaimed composers today. She is a spirited, compelling, and sensitive composer whose music enhances the poetry of America's most prominent authors. Notable among her works are song cycles for soprano based on the poetry of female writers, among them novelist and poet Willa Cather (1873-1947). Larsen has produced two song cycles on works from Cather's substantial output of fiction: one based on Cather's short story, "Eric Hermannson's Soul," titled Margaret Songs: Three Songs from Willa Cather (1996); and later, My Antonia (2000), based on Cather's novel of the same title. In Margaret Songs, Cather's poetry and short stories--specifically the character of Margaret Elliot--combine with Larsen's unique compositional style to create a surprising collaboration. This study explores how Larsen in these songs delves into the emotional and psychological depths of Margaret's character, not fully formed by Cather. It is only through Larsen's music and Cather's poetry that Margaret's journey through self-discovery and love become fully realized. This song cycle is a glimpse through the eyes of two prominent female artists on the societal pressures placed upon Margaret's character, many of which still resonate with women in today's culture. This study examines the work Margaret Songs by discussing Willa Cather, her musical influences, and the conditions surrounding the writing of "Eric Hermannson's Soul." It looks also into Cather's influence on Libby Larsen and the commission leading to Margaret Songs. Finally, a description of the musical, dramatic, and textual content of the songs completes this interpretation of the interactions of Willa Cather, Libby Larsen, and the character of Margaret Elliot.
ContributorsMcLain, Christi Marie (Author) / FitzPatrick, Carole (Thesis advisor) / Dreyfoos, Dale (Committee member) / Holbrook, Amy (Committee member) / Ryan, Russell (Committee member) / Arizona State University (Publisher)
Created2013
Discovering Puerto Rican art song: a research project on four art song works by Héctor Campos Parsi
Description
Puerto Rico has produced many important composers who have contributed to the musical culture of the nation during the last 200 years. However, a considerable amount of their music has proven to be difficult to access and may contain numerous errors. This research project intends to contribute to the accessibility of such music and to encourage similar studies of Puerto Rican music. This study focuses on the music of Héctor Campos Parsi (1922-1998), one of the most prominent composers of the 20th century in Puerto Rico. After an overview of the historical background of music on the island and the biography of the composer, four works from his art song repertoire are given for detailed examination. A product of this study is the first corrected edition of his cycles Canciones de Cielo y Agua, Tres Poemas de Corretjer, Los Paréntesis, and the song Majestad Negra. These compositions date from 1947 to 1959, and reflect both the European and nationalistic writing styles of the composer during this time. Data for these corrections have been obtained from the composer's manuscripts, published and unpublished editions, and published recordings. The corrected scores are ready for publication and a compact disc of this repertoire, performed by soprano Melliangee Pérez and the author, has been recorded to bring to life these revisions. Despite the best intentions of the author, the various copyright issues have yet to be resolved. It is hoped that this document will provide the foundation for a resolution and that these important works will be available for public performance and study in the near future.
ContributorsRodríguez Morales, Luis F., 1980- (Author) / Campbell, Andrew (Thesis advisor) / Buck, Elizabeth (Committee member) / Holbrook, Amy (Committee member) / Kopta, Anne (Committee member) / Ryan, Russell (Committee member) / Arizona State University (Publisher)
Created2013
ContributorsYi, Joyce (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-22
ContributorsCummiskey, Hannah (Performer) / Kim, Olga (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-23
ContributorsEvans, Emily (Performer) / Sherrill, Amanda (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-02
ContributorsMartorana, Gabrielle (Performer) / Olarte, Aida (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-20
ContributorsBan, Banlingyu (Performer) / ASU Library. Music Library (Publisher)
Created2018-04-10
Description
Our goal was to design a method to express soluble folded major histocompatibility complex (MHC) proteins using human cell line HeLa lysate with the novel 1-Step Human In Vitro Protein Expression by Thermo Scientific in the presence of β2 microglobulin (β2m) and antigenic peptide.
We confirmed that the soluble protein MHC-A2.1 could be successfully attached to the Luminex magnetic beads and detected using the primary antibody anti-GST and the detection antibody goat mAb mouse PE. The average net MFI of the attached pA2.1-bead complex was 8182. Biotinylated A2.1 MHC complexes pre-folded with β2m and FLU M1 peptide (A2.1 monomers) were also successfully attached to Luminex magnetic beads and detected with BB7.2. The average net MFI of the detected A2.1 monmer-bead complexes was 318. The protein MHC complexes were multimerized on magnetic beads to create MHC tetramers and detected with BB7.2, PE labeled monoclonal antibody, via median fluorescent intensity with the Luminex platform. Varying protein, β2 microglobulin (β2m), and peptide concentrations were tested in a number of MHC-A2.1 protein refolding trials. Different antigenic peptides and attachment methods were also tested. However, none of the MHC-A2.1 protein folding and capture trials were successful. Although MHC-A2.1 complexes and recombinant MHC molecules could be attached to Luminex magnetic beads and be detected by Luminex arrays, soluble protein A2.1 could not be successfully expressed, refolded, captured onto Luminex beads, and detected. All refolding trials resulted in a net MFI of <25. The failed refolding and capture trials of A2.1 lead to the conclusion that human cell line HeLa lysate cannot be used to properly fold MHC molecules. However, efforts to refold the complexes onto Luminex magnetic beads are ongoing. We are also using the baculovirus expression system to refold soluble A2.1 lysate onto peptide-bead complexes.
We confirmed that the soluble protein MHC-A2.1 could be successfully attached to the Luminex magnetic beads and detected using the primary antibody anti-GST and the detection antibody goat mAb mouse PE. The average net MFI of the attached pA2.1-bead complex was 8182. Biotinylated A2.1 MHC complexes pre-folded with β2m and FLU M1 peptide (A2.1 monomers) were also successfully attached to Luminex magnetic beads and detected with BB7.2. The average net MFI of the detected A2.1 monmer-bead complexes was 318. The protein MHC complexes were multimerized on magnetic beads to create MHC tetramers and detected with BB7.2, PE labeled monoclonal antibody, via median fluorescent intensity with the Luminex platform. Varying protein, β2 microglobulin (β2m), and peptide concentrations were tested in a number of MHC-A2.1 protein refolding trials. Different antigenic peptides and attachment methods were also tested. However, none of the MHC-A2.1 protein folding and capture trials were successful. Although MHC-A2.1 complexes and recombinant MHC molecules could be attached to Luminex magnetic beads and be detected by Luminex arrays, soluble protein A2.1 could not be successfully expressed, refolded, captured onto Luminex beads, and detected. All refolding trials resulted in a net MFI of <25. The failed refolding and capture trials of A2.1 lead to the conclusion that human cell line HeLa lysate cannot be used to properly fold MHC molecules. However, efforts to refold the complexes onto Luminex magnetic beads are ongoing. We are also using the baculovirus expression system to refold soluble A2.1 lysate onto peptide-bead complexes.
ContributorsChang, Peter S (Author) / Anderson, Karen (Thesis director) / Chang, Yung (Committee member) / Sundaresan, Krishna (Committee member) / Barrett, The Honors College (Contributor) / T. Denny Sanford School of Social and Family Dynamics (Contributor) / Department of Chemistry and Biochemistry (Contributor)
Created2013-05