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- All Subjects: Clarinet and piano music
Description
Despite the wealth of folk music traditions in Portugal and the importance of the clarinet in the music of bandas filarmonicas, it is uncommon to find works featuring the clarinet using Portuguese folk music elements. In the interest of expanding this type of repertoire, three new works were commissioned from three different composers. The resulting works are Seres Imaginarios 3 by Luis Cardoso; Delirio Barroco by Tiago Derrica; and Memória by Pedro Faria Gomes. In an effort to submit these new works for inclusion into mainstream performance literature, the author has recorded these works on compact disc. This document includes interview transcripts with each composer, providing first-person discussion of each composition, as well as detailed biographical information on each composer. To provide context, the author has included a brief discussion on Portuguese folk music, and in particular, the role that the clarinet plays in Portuguese folk music culture.
ContributorsFerreira, Wesley (Contributor) / Spring, Robert S (Thesis advisor) / Bailey, Wayne (Committee member) / Gardner, Joshua (Committee member) / Hill, Gary (Committee member) / Schuring, Martin (Committee member) / Solis, Theodore (Committee member) / Arizona State University (Publisher)
Created2013
ContributorsBurton, Charlotte (Performer) / ASU Library. Music Library (Publisher)
Created2018-04-08
ContributorsDruesedow, Elizabeth (Performer) / ASU Library. Music Library (Publisher)
Created2018-04-07
Description
Protein AMPylation is a recently discovered and relatively unstudied post-translational modification (PTM). AMPylation has previously been shown to play an important role in metabolic regulation and host pathogenesis in bacteria, but the recent identification of potential AMPylators across many species in every domain of life has supported the possibility that AMPylation could be a more fundamental and physiologically significant regulatory PTM. For the first time, we characterized the auto-AMPylation capability of the human protein SOS1 through in vitro AMPylation experiments using full-length protein and whole-domain truncation mutants. We found that SOS1 can become AMPylated at a tyrosine residue possibly within the Cdc25 domain of the protein, the Dbl homology domain is vital for efficient auto-AMPylation activity, and the C-terminal proline-rich domain exhibits a complex regulatory function. The proline-rich domain alone also appears to be capable of catalyzing a separate, unidentified covalent self-modification using a fluorescent ATP analogue. Finally, SOS1 was shown to be capable of catalyzing the AMPylation of two endogenous human protein substrates: a ubiquitous, unidentified protein of ~49kDa and another breast-cancer specific, unidentified protein of ~28kDa.
ContributorsOber-Reynolds, Benjamin John (Author) / LaBaer, Joshua (Thesis director) / Borges, Chad (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor) / School of Life Sciences (Contributor)
Created2014-05
Description
AMPylation is a post-translation modification that has an important role in the survival of many bacterial pathogens by affecting the host cell's molecular signaling. In the course of studying this intercellular manipulation, there has only been modest progression in the identification of the enzymes with AMPylation capabilities (AMPylators) and their respective targets. The reason for these minimal developments is the inability to analyze a large subset of these proteins. Therefore, to increase the efficiency of the identification and characterization of the proteins, Yu et al developed a high-throughput non-radioactive discovery platform using Human Nucleic Acid Programmable Protein Arrays (NAPPA) and a validation platform using bead-based assays. The large-scale unbiased screening of potential substrates for two bacterial AMPylators containing Fic domain, VopS and IbpAFic2, had been performed and dozens of novel substrates were identified and confirmed. With the efficiency of this method, the platform was extended to the identification of novel substrates for a Legionella virulence factor, SidM, containing a different adenylyl transferase domain. The screening was performed using NAPPA arrays comprising of 10,000 human proteins, the active AMPylator SidM, and its inactive D110/112A mutant as a negative control. Many potential substrates of SidM were found, including Rab GTPases and non-GTPase proteins. Several of which have been confirmed with the bead-based AMPylation assays.
ContributorsGraves, Morgan C. (Author) / LaBaer, Joshua (Thesis director) / Qiu, Ji (Committee member) / Yu, Xiaobo (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor)
Created2013-05
Description
This project includes a recording and performance guide for three newly commissioned pieces for the clarinet. The first piece, shimmer, was written by Grant Jahn and is for B-flat clarinet and electronics. The second piece, Paragon, is for B-flat clarinet and piano and was composed by Dr. Theresa Martin. The third and final piece, Duality in the Eye of a Bovine, was written by Kurt Mehlenbacher and is for B-flat clarinet, bass clarinet, and piano. In addition to the performance guide, this document also includes background information and program notes for the compositions, as well as composer biographical information, a list of other works featuring the clarinet by each composer, and transcripts of composer and performer interviews. This document is accompanied by a recording of the three pieces.
ContributorsPoupard, Caitlin Marie (Author) / Spring, Robert (Thesis advisor) / Gardner, Joshua (Thesis advisor) / Hill, Gary (Committee member) / Oldani, Robert (Committee member) / Schuring, Martin (Committee member) / Arizona State University (Publisher)
Created2016
Description
The primary objective of this research project is to expand the clarinet repertoire with the addition of four new pieces. Each of these new pieces use contemporary clarinet techniques, including electronics, prerecorded sounds, multiphonics, circular breathing, multiple articulation, demi-clarinet, and the clari-flute. The repertoire composed includes Grant Jahn’s Duo for Two Clarinets, Reggie Berg’s Funkalicious for Clarinet and Piano, Rusty Banks’ Star Juice for Clarinet and Fixed Media, and Chris Malloy’s A Celestial Breath for Clarinet and Electronics. In addition to the musical commissions, this project also includes interviews with the composers indicating how they wrote these works and what their influences were, along with any information pertinent to the performer, professional recordings of each piece, as well as performance notes and suggestions.
ContributorsCase-Ruchala, Celeste Ann (Contributor) / Gardner, Joshua (Thesis advisor) / Spring, Robert (Thesis advisor) / Hill, Gary (Committee member) / Rogers, Rodney (Committee member) / Schuring, Martin (Committee member) / Arizona State University (Publisher)
Created2016
ContributorsClements, Katrina (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-15
ContributorsClifton-Armenta, Tyler (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-16
Description
Many Fic domain proteins, through catalyzing post translational modifications (PTM) of protein substrates, functionally contribute to bacterial pathogenesis and the regulation of bacterial growth. Furthermore, one form of Fic-mediated regulation is the Fic toxin-antitoxin system, whereby an antitoxin interacts with and inhibits the Fic toxin. This study sought to determine the functional importance of Mycobacterium tuberculosis Fic and its putative antitoxin protein, Rv3642c. Using M. tuberculosis H37Rv genetic deletion mutants, fic and Rv3642c were demonstrated to promote intracellular survival in human THP-1 macrophage-like cells. Unlike other Fic toxins, of Fic toxin-antitoxin systems, Fic did not inhibit bacterial growth in vitro in the absence of Rv3642c. Notably, Fic demonstrated in vitro AMPylation of a THP-1 cell extract protein as shown by immunodetection. Fic also exhibited auto-AMPylation activity. Interestingly, a mutation of the conserved histidine in the Fic domain motif, a residue previously shown to be critical for AMPylation, had no effect on Fic-mediated ATP hydrolysis or AMPylation activity. Rv3642c was demonstrated to form a complex with Fic when co-expressed in Escherichia coli, indicating a toxin-antitoxin interaction. Screening M. tuberculosis protein fractions and culture filtrate with α-Fic and α-Rv3642c rabbit antisera did not detect monomers of Fic or Rv3642c, thus the cellular localization of Fic and the Rv3642c-Fic complex remains unclear. The results of this study provide insight into the function of M. tuberculosis Fic, and suggest that Fic and Rv3642c are important for M. tuberculosis survival in the intracellular macrophage environment. Furthermore, these findings challenge the current dogma that Fic domain catalysis is dependent on the conserved histidine of the Fic motif.
ContributorsLaMarca, Ryan (Author) / Haydel, Shelley (Thesis advisor) / Lake, Douglas (Committee member) / Nickerson, Cheryl (Committee member) / Arizona State University (Publisher)
Created2017