African-American Composers for the Concert Saxophone: A Look at Three Prolific Composers

African-American composers within the field of classical music have made very profound contributions to the literature. In the field of chamber music, Scott Joplin, William Grant Still, Adolphus Hailstork and other composers illustrious composers have created an established and well-documented body of repertoire for many orchestral wind instruments. The saxophone repertoire, however, has not been developed as fully due to its limited tradition as an orchestral instrument and its prominence in the tradition of jazz and popular music. African-American composers in particular appear to be significantly under-represented within the standard concert saxophone literature. My personal experiences with saxophone repertoire in academic settings, solo recitals, conferences and in surveys of standard repertoire from nationally-recognized saxophone teachers support this assertion. There are many African-American composers who have made substantial contributions to the body of repertoire for the concert saxophone. This dissertation examines the works of three prolific African-American composers for the concert saxophone; Dr. Yusef A. Lateef, Andrew N. White III, and Dr. David N. Baker. All have composed more than five separate works featuring the concert saxophone. This project comprises three recitals, each dedicated to one of the three composers selected for this dissertation. Each recital presented will present their compositions featuring the saxophone as a soloist with various types of accompaniment. The project also includes newly-created piano reductions of Dr. David Baker's works for saxophone and orchestra made collaboratively with Baker and arranger John Leszczynski.

Coarse Graining to Invesitigate Peptide-Lipid Interactions

Experimental characterization of molecular details is challenging, and although single molecule experiments have gained prominence, oligomer characterization remains largely unexplored. The ability to monitor the time evolution of individual molecules while they self assemble is essential in providing mechanistic insights about biological events. Molecular dynamics (MD) simulations can fill the gap in knowledge between single molecule experiments and ensemble studies like NMR, and are increasingly used to gain a better understanding of microscopic properties. Coarse-grained (CG) models aid in both exploring longer length and time scale molecular phenomena, and narrowing down the key interactions responsible for significant system characteristics. Over the past decade, CG techniques have made a significant impact in understanding physicochemical processes. However, the realm of peptide-lipid interfacial interactions, primarily binding, partitioning and folding of amphipathic peptides, remains largely unexplored compared to peptide folding in solution. The main drawback of existing CG models is the inability to capture environmentally sensitive changes in dipolar interactions, which are indigenous to protein folding, and lipid dynamics. We have used the Drude oscillator approach to incorporate structural polarization and dipolar interactions in CG beads to develop a minimalistic peptide model, WEPPROM (Water Explicit Polarizable PROtein Model), and a lipid model WEPMEM (Water Explicit Polarizable MEmbrane Model). The addition of backbone dipolar interactions in a CG model for peptides enabled us to achieve alpha-beta secondary structure content de novo, without any added bias. As a prelude to studying amphipathic peptide-lipid membrane interactions, the balance between hydrophobicity and backbone dipolar interactions in driving ordered peptide aggregation in water and at a hydrophobic-hydrophilic interface, was explored. We found that backbone dipole interactions play a crucial role in driving ordered peptide aggregation, both in water and at hydrophobic-hydrophilic interfaces; while hydrophobicity is more relevant for aggregation in water. A zwitterionic (POPC: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) and an anionic lipid (POPS: 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine) are used as model lipids for WEPMEM. The addition of head group dipolar interactions in lipids significantly improved structural, dynamic and dielectric properties of the model bilayer. Using WEPMEM and WEPPROM, we studied membrane-induced peptide folding of a cationic antimicrobial peptide with anticancer activity, SVS-1. We found that membrane-induced peptide folding is driven by both (a) cooperativity in peptide self interaction and (b) cooperativity in membrane-peptide interactions. The dipolar interactions between the peptide and the lipid head-groups contribute to stabilizing folded conformations. The role of monovalent ion size and peptide concentration in driving lipid domain formation in anionic/zwitterionic lipid mixtures was also investigated. Our study suggest monovalent ion size to be a crucial determinant of interaction with lipid head groups, and hence domain formation in lipid mixtures. This study reinforces the role of dipole interactions in protein folding, lipid membrane properties, membrane induced peptide folding and lipid domain formation. Therefore, the models developed in this thesis can be used to explore a multitude of biomolecular processes, both at longer time-scales and larger system sizes.

KNOWING THE ENEMY: NAZI FOREIGN INTELLIGENCE IN WAR, HOLOCAUST, AND POSTWAR

“Knowing the Enemy: Nazi Foreign Intelligence in War, Holocaust and Postwar,” reveals the importance of ideologically-driven foreign intelligence reporting in the wartime radicalization of the Nazi dictatorship, and the continued prominence of Nazi discourses in postwar reports from German intelligence officers working with the U.S. Army and West German Federal Intelligence Service after 1945. For this project, I conducted extensive archival research in Germany and the United States, particularly in overlooked and files pertaining to the wartime activities of the Reichssicherheitshauptamt, Abwehr, Fremde Heere Ost, Auswärtiges Amt, and German General Staff, and the recently declassified intelligence files pertaining to the postwar activities of the Gehlen Organization, Bundesnachrichtendienst, and Foreign Military Studies Program. Applying the technique of close textual analysis to the underutilized intelligence reports themselves, I discovered that wartime German intelligence officials in military, civil service, and Party institutions all lent the appearance of professional objectivity to the racist and conspiratorial foreign policy beliefs held in the highest echelons of the Nazi dictatorship. The German foreign intelligence services’ often erroneous reporting on Great Britain, the Soviet Union, the United States, and international Jewry simultaneously figured in the radicalization of the regime’s military and anti-Jewish policies and served to confirm the ideological preconceptions of Hitler and his most loyal followers. After 1945, many of these same figures found employment with the Cold War West, using their “expertise” in Soviet affairs to advise the West German Government, U.S. Military, and CIA on Russian military and political matters. I chart considerable continuities in personnel and ideas from the wartime intelligence organizations into postwar West German and American intelligence institutions, as later reporting on the Soviet Union continued to reproduce the flawed wartime tropes of innate Russian military and racial inferiority.