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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
Description
Photosystem I (PSI) is a multi-subunit, pigment-protein complex that catalyzes light-driven electron transfer (ET) in its bi-branched reaction center (RC). Recently it was suggested that the initial charge separation (CS) event can take place independently within each ec2/ec3 chlorophyll pair. In order to improve our understanding of this phenomenon, we have generated new mutations in the PsaA and PsaB subunits near the electron transfer cofactor 2 (ec2 chlorophyll). PsaA-Asn604 accepts a hydrogen bond from the water molecule that is the axial ligand of ec2B and the case is similar for PsaB-Asn591 and ec2A. The second set of targeted sites was PsaA-Ala684 and PsaB-Ala664, whose methyl groups are present near ec2A and ec2B, respectively. We generated a number of mutants by targeting the selected protein residues. These mutations were expected to alter the energetics of the primary charge separation event.
The PsaA-A684N mutants exhibited increased ET on the B-branch as compared to the A-branch in both in vivo and in vitro conditions. The transient electron paramagnetic resonance (EPR) spectroscopy revealed the formation of increased B-side radical pair (RP) at ambient and cryogenic temperatures. The ultrafast transient absorption spectroscopy and fluorescence decay measurement of the PsaA-A684N and PsaB-A664N showed a slight deceleration of energy trapping. Thus making mutations near ec2 on each branch resulted into modulation of the charge separation process. In the second set of mutants, where ec2 cofactor was target by substitution of PsaA-Asn604 or PsaB-Asn591 to other amino acids, a drop in energy trapping was observed. The quantum yield of CS decreases in Asn to Leu and His mutants on the respective branch. The P700 triplet state was not observed at room and cryogenic temperature for these mutants, nor was a rapid decay of P700+ in the nanosecond timescale, indicating that the mutations do not cause a blockage of electron transfer from the ec3 Chl. Time-resolved fluorescence results showed a decrease in the lifetime of the energy trapping. We interpret this decrease in lifetime as a new channel of excitation energy decay, in which the untrapped energy dissipates as heat through a fast internal conversion process. Thus, a variety of spectroscopic measurements of PSI with point mutations near the ec2 cofactor further support that the ec2 cofactor is involved in energy trapping process.
The PsaA-A684N mutants exhibited increased ET on the B-branch as compared to the A-branch in both in vivo and in vitro conditions. The transient electron paramagnetic resonance (EPR) spectroscopy revealed the formation of increased B-side radical pair (RP) at ambient and cryogenic temperatures. The ultrafast transient absorption spectroscopy and fluorescence decay measurement of the PsaA-A684N and PsaB-A664N showed a slight deceleration of energy trapping. Thus making mutations near ec2 on each branch resulted into modulation of the charge separation process. In the second set of mutants, where ec2 cofactor was target by substitution of PsaA-Asn604 or PsaB-Asn591 to other amino acids, a drop in energy trapping was observed. The quantum yield of CS decreases in Asn to Leu and His mutants on the respective branch. The P700 triplet state was not observed at room and cryogenic temperature for these mutants, nor was a rapid decay of P700+ in the nanosecond timescale, indicating that the mutations do not cause a blockage of electron transfer from the ec3 Chl. Time-resolved fluorescence results showed a decrease in the lifetime of the energy trapping. We interpret this decrease in lifetime as a new channel of excitation energy decay, in which the untrapped energy dissipates as heat through a fast internal conversion process. Thus, a variety of spectroscopic measurements of PSI with point mutations near the ec2 cofactor further support that the ec2 cofactor is involved in energy trapping process.
ContributorsBadshah, Syed Lal (Author) / Redding, Kevin E (Thesis advisor) / Fromme, Petra (Committee member) / Gould, Ian (Committee member) / Arizona State University (Publisher)
Created2014
Description
Photochromic molecules, which photoisomerize between two chemically and optically distinct states, are well suited for electron and energy transfer to covalently attached chromophores. This dissertation aims to manipulate electron and energy transfer by photochromic control in a number of organic molecular systems. Herein the synthesis, characterization and function of these organic molecular systems will be described. Electron and energy transfer were quantified by the use of steady state absorbance and fluorescence, as well as time-resolved fluorescence and transient absorbance. A dithienylethene-porphrin-fullerene triad was synthesized to investigate photochromic control of photo-induced electron transfer. Control of two distinct electron transfer pathways was achieved by photochromic switching. A molecular dyad was synthesized, in which fluorescence was modulated by energy transfer by photoinduced isomerization. Also described is a triplet-triplet annihilation upconversion system that covalently attaches fluorophores to improve quantum yield. Overall these studies demonstrate complex molecular switching systems, which may lead to advancement in organic electronic applications and organic based artificial photosynthesis systems.
ContributorsCrisman, Jeffrey (Author) / Gust, John D (Thesis advisor) / Rose, Seth (Committee member) / Moore, Ana (Committee member) / Arizona State University (Publisher)
Created2014
Description
The photosynthetic reaction center is a type of pigment-protein complex found widely in photosynthetic bacteria, algae and higher plants. Its function is to convert the energy of sunlight into a chemical form that can be used to support other life processes. The high efficiency and structural simplicity make the bacterial reaction center a paradigm for studying electron transfer in biomolecules. This thesis starts with a comparison of the primary electron transfer process in the reaction centers from the Rhodobacter shperoides bacterium and those from its thermophilic homolog, Chloroflexus aurantiacus. Different temperature dependences in the primary electron transfer were found in these two type of reaction centers. Analyses of the structural differences between these two proteins suggested that the excess surface charged amino acids as well as a larger solvent exposure area in the Chloroflexus aurantiacus reaction center could explain the different temperature depenence. The conclusion from this work is that the electrostatic interaction potentially has a major effect on the electron transfer. Inspired by these results, a single point mutant was designed for Rhodobacter shperoides reaction centers by placing an ionizable amino acid in the protein interior to perturb the dielectrics. The ionizable group in the mutation site largely deprotonated in the ground state judging from the cofactor absorption spectra as a function of pH. By contrast, a fast charge recombination assoicated with protein dielectric relaxation was observed in this mutant, suggesting the possibility that dynamic protonation/deprotonation may be taking place during the electron transfer. The fast protein dielectric relaxation occuring in this mutant complicates the electron transfer pathway and reduces the yield of electron transfer to QA. Considering the importance of the protein dielectric environment, efforts have been made in quantifying variations of the internal field during charge separation. An analysis protocol based on the Stark effect of reaction center cofactor spectra during charge separation has been developed to characterize the charge-separated radical field acting on probe chromophores. The field change, monitored by the dynamic Stark shift, correlates with, but is not identical to, the electron transfer kinetics. The dynamic Stark shift results have lead to a dynamic model for the time-dependent dielectric that is complementary to the static dielectric asymmetry observed in past steady state experiments. Taken together, the work in this thesis emphasizes the importance of protein electrostatics and its dielectric response to electron transfer.
ContributorsGuo, Zhi (Author) / Woodbury, Neal W (Thesis advisor) / Lindsay, Stuart M (Committee member) / Ross, Robert (Committee member) / Ozkan, Banu S (Committee member) / Moore, Thomas A. (Committee member) / Arizona State University (Publisher)
Created2012
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