This thesis presents four studies investigating (1) whether incidentally primed control-related words can attenuate the impact of activated stereotypes on subsequent evaluation of a target person, (2) the impact of motivated forgetting on the recall of stereotypically congruent and incongruent information, and (3) the impact of a directed forgetting instruction on the false recall and recognition of nonpresented stereotypical information. In three experiments, Study I showed that participants initially primed with the social category, immigrant, and subsequently primed with words that were evocative of control or self-control made less negative impression of a target displaying ambiguous behaviors than participants not exposed to such words. Study II, using a directed-forgetting paradigm, demonstrated in two experiments that participants subliminally primed with Swedish facial photographs who later studied stereotypically incongruent words roughly recalled an equal number of items regardless of the forget or remember instructions. Study III showed that participants primed with the social category, immigrant and then studied a list of stereotypically related and unrelated words falsely recognized more nonpresented stereotypical words when they were furnished with a forget than a remember instruction. Similarly, Study IV (Experiment 2) demonstrated that participants primed with the social category, immigrant, but not with a neutral category, falsely recalled more nonpresented stereotypical words when their cognitive capacity was depleted through a concurrent memory load task. The thesis presents a review and a discussion of some of the theoretical underpinnings of the extant literature on stereotyping and intergroup relations and of the social implications of the present findings.

The sun provides us daily with large quantities of energy in the form of light. With the world’s increasing demand of electrical energy the prospect of converting this solar light into electricity is highly tempting. In the strive towards mass-production and low cost solar cells, new types of solar cells are being developed, e.g. solar cells completely based on organic molecules and polymers. These materials offer a promising potential of low cost and large scale manufacturing and have the additional advantage that they can be produced on flexible and light weight substrate which opens for new and innovating application areas, e.g. integration with paper or textiles, or as building materials. In polymer solar cells a combination of two materials are used, an electron donor and an electron acceptor. The three dimensional distribution of the donor and acceptor in the active layer of the device, i.e. the morphology, is known to have larger influence of the solar cell performance. For the optimal morphology there is a trade-off between sometimes conflicting criteria for the various steps of the energy conversion process. The dissociation of photogenerated excitons takes place at an interface between the donor and acceptor materials. Therefore an efficient generation of charges requires a large interface between the two components. However, for charge transport and collection at the electrodes, continuous pathways for the charges to the electrodes are required. In this thesis, results from morphology studies by atomic force microscopy (AFM) and dynamic secondary ion mass spectrometry (SIMS) of spin-coated blend and bilayer thin films of polyfluorene co-polymers, especially poly[(9,9-dioctylfluorenyl-2,7-diyl)-co-5,5-(4´,7´-di-2-thienyl-2´,1´,3´-benzothiadiazole)] APFO-3, and the fullerene derivative [6,6]-phenyl-C61-butyric acid methyl ester (PCBM) are presented. It is shown that by varying the blend ratio, the spin.-coating solvent, and/or the substrate, different morphologies can be obtained, e.g. diffuse bilayer structures, spontaneously formed multilayer structures and homogeneous blends. The connection between these different morphologies and the performance of solar cells is also analysed. The results indicate that nano-scale engineering of the morphology in the active layer may be an important factor in the optimization of the performance of polymer solar cells.

AcrA is the periplasmic component of an efflux system AcrA-AcrB-TolC, which can expel different classes of antibiotics. AcrB is the inner membrane (IM) pump that utilizes proton-motive force for the active transport, TolC is the outer membrane (OM) channel, and AcrA coordinates the actions of AcrB and TolC, so that substrates are expelled across the two membranes, bypassing the periplasm. It has been proposed that AcrA either provides a static seamless link between AcrB and TolC, or acts like its analogous viral membrane fusion protein (MFP) and actively brings the IM and OM closer for substrate transfer. To better understand the role of AcrA in the efflux mechanism, site-directed spin labeling (SDSL)/EPR (electron paramagnetic resonance) spectroscopy is used to investigate the structure and dynamics of AcrA in solution. My results demonstrated that AcrA is a dynamic protein that undergoes pH-dependent and reversible conformational changes. AcrA contains an interrupted alpha-helical, coiled-coil domain flanked by a pair of beta-stranded lipoyl motifs, and my SDSL/EPR analysis revealed that the pH-induced conformation change mainly involves the coiled-coil and the lipoyl domains. In addition, I found that each AcrA monomer folds into an intra-molecular hairpin and AcrA monomers oligomerize with their coiled-coil hairpins aligned in parallel. Unlike the pH-induced conformational rearrangement of a viral MFP, change in pH alters both intra- and inter-molecular interaction along the coiled-coil of AcrA without rearranging the hairpin fold. The organization of AcrA protomers and its pH-induced conformational switching are, however, congruent with the TolC coiled-coil hairpins in the iris-like opening of the TolC channel. Together, my studies suggest that rather than being a passive structural linkage between AcrB and TolC, AcrA plays an active role mediating the drug efflux. The reported AcrA dynamics provides new insights into the AcrA-TolC interactions for the channel opening during the efflux process.

ABSTRACT Protein-protein interactions play a central role in most biological processes. One such biological process is the maintenance of a reducing environment inside the cell. To maintain an internal reducing environment, living cells have evolved two enzymatic systems (glutathione and thioredoxin (Trx) systems). The Trx system is composed of the enzyme TrxR and its substrate Trx. The two proteins constitute an important thiol-dependent redox system that catalyzes the reduction of many proteins that are responsible for a variety of cellular functions. The system relies on transient protein-protein interactions between Trx and TrxR for its function. Cross-reactivity of components of the Trx system between species has been shown to be medically relevant. For example, Helicobacter pylori Trx (HP Trx) is thought to mediate catalytic reduction of human immunoglobulins and thus facilitate immune evasion. It has also been proposed that Helicobacter pylori gains access to the impenetrable gastric mucous layer by using secreted HP Trx to reduce the disulfide bonds present in the cysteine-rich mucin regions that are responsible for cross-linking mucin monomers. Therefore, disruption of secreted HP Trx-host protein interaction may result in restoration of the viscoelastic and hydrophobic protective properties of mucus. Previous studies aimed at understanding the nature of cross-reactivity of Trx system components among various species have shown that Trxs have higher affinity for cognate TrxRs (same species), than for TrxRs from different species. However, the basis for this specificity is not known. A growing body of evidence suggests that most protein-protein interactions are mediated by a small number of protein-protein interface residues, referred to as hot spot residues or binding epitopes. Therefore, understanding the biochemical basis of the affinity of proteins for their partners usually begins by identifying the hot spot residues responsible for the protein complex interactions. In this study, the crystal structures of Deinococcus radiodurans thioredoxin reductase (DR TrxR) and Helicobacter pylori TrxR (HP TrxR) were determined at 1.9 Å and 2.4 Å respectively. Analysis of the Trx-binding sites of both structures suggests that the basis of affinity and specificity of Trx for TrxR is primarily due to the shape rather than the charge of the surface. In addition, the complex between Escherichia coli thioredoxin reductase (EC TrxR) and its substrate thioredoxin (EC Trx) was used to identify residues that are responsible for TrxR-Trx interface stability. Using computational alanine scanning mutagenesis and visual inspection of the EC TrxR-Trx interface, 22 EC TrxR side chains were shown to make contact across the TrxR-Trx interface. Although more than 20 EC TrxR side chains make contact across the TrxR-Trx interface, our results suggest that only 4 residues (F81, R130, F141, and F142) account for the majority of the EC TrxR-Trx interface stability. Individual replacement of equivalent DR TrxR residues (M84, K137, F148, F149) with alanine resulted in drastic changes in binding affinity, confirming that the four residues account for most of TrxR-Trx interface stability. These hot spot residues are surrounded by less important residues (hydrophobic and hydrophilic) that are also predicted to contribute to interface stability. F148 and F149 are invariant across bacterial TrxRs, however other residues that contact Trx are less conserved including M84 and K137. When M84 and K137 were changed to match equivalent E. coli TrxR residues (K137R, M84F); D. radiodurans TrxR substrate specificity was altered from its own Trx to that of E. coli Trx. The results suggest that a small subset of the TrxR-Trx interface residues are responsible for the majority of Trx binding affinity and specificity, a property that has been shown to general to protein-protein interfaces.

During the summer of 1968, the Vice President for Student Affairs at Ball State University, established the Office of Special Programs. Personnel of the Office were charged with the responsibility for developing and providing special services for students with low academic records so that collegiate success and persistence might be enhanced. The Director of Special Programs was directly charged with the responsibility for providing academic counseling, advice relative to course selections, and for marshalling existing university academic and ancillary support systems as necessary to improve college persistence behaviors among students classified for "Admission with Warning."Personnel of the Office of Special Programs developed and implemented a program designed to provide special academic and supportive services to "Admission with Warning" students. The Directed Admission Student Experimental Program was implemented in the fall of 1968. The program included a remedial reading course, a remedial writing course designed specifically for students identified for the DASEP experience. Personal counseling and special Curricular Advising services were provided to all DASEP students. Over the period from 1968-1972 a total of 274 students were selected to be participants in the DASEP group, and a total of 273 students were identified for inclusion in a control group.The purpose of this study was to determine whether students admitted to the Ball State University Directed Admission Student Experimental Program (DASEP) during the period from 1968 to 1972, persisted to program completion more frequently than did similar students in an identical non-DASEP control group. If the null hypothesis relating to the major purpose was not accepted, differences among DASEP persisters and non-persisters would be investigated.A second purpose of the study was to collect and analyze evaluative perceptions from participants of the Directed Admission Student. Experimental Program relative to the special services provided.The research was planned to test the null hypothesis relating to persistence in the DASEP program and to secure evaluative perceptions about the services from 274 DASEP students.The investigator collected data on persistence in the DASEP program from 265 DASEP and 255 control group students. Data were statistically treated by means of the chi square statistic. The .05 level was used for hypothesis acceptance or non-acceptance. In order to secure evaluative perceptions about services provided participants in the DASEP program, a Likert type instrument was developed and sent to 250 participants in the DASEP program. Review of the data led to the following conclusions:There was no statistically significant difference found between the DASEP group and control group students in persistence to the completion of their individual educational program.Less than one-half of the DASEP students perceived the services provided by the Reading Clinic to be helpful.Slightly more than one-half perceived the services of the Writing Clinic to be helpful.Depending upon the service, about one-half of the students perceived the special Curricular Advising services to be helpful.About one-third perceived the subjects taught in the seminar class to be helpful.Slightly less than one-half of the DASEP students perceived counseling, provided by the staff of Special Programs to be helpful.In a summary question, 94 percent of the DASEP students perceived the DASEP program had been beneficial to them.

AcrA is the periplasmic component of an efflux system AcrA-AcrB-TolC, which can expel different classes of antibiotics. AcrB is the inner membrane (IM) pump that utilizes proton-motive force for the active transport, TolC is the outer membrane (OM) channel, and AcrA coordinates the actions of AcrB and TolC, so that substrates are expelled across the two membranes, bypassing the periplasm. It has been proposed that AcrA either provides a static seamless link between AcrB and TolC, or acts like its analogous viral membrane fusion protein (MFP) and actively brings the IM and OM closer for substrate transfer. To better understand the role of AcrA in the efflux mechanism, site-directed spin labeling (SDSL)/EPR (electron paramagnetic resonance) spectroscopy is used to investigate the structure and dynamics of AcrA in solution. My results demonstrated that AcrA is a dynamic protein that undergoes pH-dependent and reversible conformational changes. AcrA contains an interrupted alpha-helical, coiled-coil domain flanked by a pair of beta-stranded lipoyl motifs, and my SDSL/EPR analysis revealed that the pH-induced conformation change mainly involves the coiled-coil and the lipoyl domains. In addition, I found that each AcrA monomer folds into an intra-molecular hairpin and AcrA monomers oligomerize with their coiled-coil hairpins aligned in parallel. Unlike the pH-induced conformational rearrangement of a viral MFP, change in pH alters both intra- and inter-molecular interaction along the coiled-coil of AcrA without rearranging the hairpin fold. The organization of AcrA protomers and its pH-induced conformational switching are, however, congruent with the TolC coiled-coil hairpins in the iris-like opening of the TolC channel. Together, my studies suggest that rather than being a passive structural linkage between AcrB and TolC, AcrA plays an active role mediating the drug efflux. The reported AcrA dynamics provides new insights into the AcrA-TolC interactions for the channel opening during the efflux process.

This thesis consists of three self-contained essays dealing with different aspects of macroeconomics and political Economy. The Relative Price of Investment Goods and Sectoral Contract Dependence I develop a quantitative model to explain the relationship between TFPs at the aggregate and sector levels and contracting institutions across countries. The incomplete contract enforcement induces distortions in the production process which come from the “hold up” problem between a final goods firm and its suppliers. Because investment goods sector is more contract dependent, its productivity suffers more from the distortion. In turn, countries endowed with weaker contract enforcement institutions face higher relative prices of investment goods. A Ricardian Model of the Labor Market with Directed Search I analyze how search friction affects the allocation in a Ricardian model of the labor market. The equilibrium shows that the matching pattern is partially mixed: Some tasks are only performed by skilled workers; some are only performed by unskilled workers; the remaining tasks are performed by both skilled and unskilled workers. The mixed matching pattern implies a mismatch in equilibrium. It turns out that the reason for the mismatch has its roots in search friction. In addition, I show labor market institutions have interesting implications for the unemployment rate and mismatch. A Dynamic Analysis of the Free-rider Problem I argue that special interest groups overcome their free-rider problem thanks to distorted government policy. As policy confers monopoly privileges on a group, it can also preserve and promote group’s organization. The key to sustaining the organization of the group is a dynamic incentive: when distorted policy generates rents for a group, each member of the group wish to make contributions not just to raise their rents today; they want to sustain their cooperation so that they will be able to influence policy in the future.

In knowledge-based engineering, the inference engine plays an important part in the behaviour of the system. A flexible and adaptive execution scheme allows the designer to experiment with different modes of operation and selecting an appropriate one with respect to the initial data set and the execution goal. In this project, an extension of an existing research prototype software in the field of knowledge-based engineering will be developed, with the goal of building a reliable and easy to use dependency resolution engine that will replace a less-than-ideal current implementation of the same. A discussion will be included how the knowledge concepts and objects can be represented in an abstract mathematical form, converting at the same time the problem of dependency resolution to a more formally specified one in terms of the data abstraction proposed. Some algorithms and methods that are used to operate on the data set will be discussed from both a theoretical and programming point of view, analysing their complexity, proposing and testing their implementation. Graphical interface controls that can be used to visualize and understand easily the relations in the available knowledge base will be also demonstrated. The testing and verification of the resulting software will be presented, comparing its behaviour against reference tools serving similar purposes. Methods for validating the consistency of the knowledge base will also be discussed. Finally, the integration of the newly-developed code within the context of the prototype will be discussed, commenting on the new features and functionality gained.

Molecular chaperones help many proteins in the cell reach their native conformation. The mechanism with which they do this has been studied extensively, but has not been entirely elucidated. This work is a continuation of the study done by Laila Villebeck et al. (2007) on the conformational rearrangements in the eukaryotic protein actin in interaction with the eukaryotic chaperone TRiC. In this study the intentions were to analyze the protein MreB, a prokaryotic homologue to actin, when interacting with the prokaryotic chaperone GroEL. The purpose was to investigate if the mechanisms of GroEL and TRiC are similar. The analysis of the conformation of MreB was to be made through calculations of fluorescence resonance energy transfer (FRET) between two positions in MreB labeled with fluorescein. A MreB mutant was made through site-specific mutagenesis to enable labeling at a specific position. Another single mutant and a corresponding double mutant needed for these measurements were avaliable from earlier studies. The results from fluorescence measurements on these mutants indicated that the degree of labeling was insufficient for accurate determination of FRET. Suggestions are made on improvements of the experimental approach for future studies.

ABSTRACT Protein-protein interactions play a central role in most biological processes. One such biological process is the maintenance of a reducing environment inside the cell. To maintain an internal reducing environment, living cells have evolved two enzymatic systems (glutathione and thioredoxin (Trx) systems). The Trx system is composed of the enzyme TrxR and its substrate Trx. The two proteins constitute an important thiol-dependent redox system that catalyzes the reduction of many proteins that are responsible for a variety of cellular functions. The system relies on transient protein-protein interactions between Trx and TrxR for its function. Cross-reactivity of components of the Trx system between species has been shown to be medically relevant. For example, Helicobacter pylori Trx (HP Trx) is thought to mediate catalytic reduction of human immunoglobulins and thus facilitate immune evasion. It has also been proposed that Helicobacter pylori gains access to the impenetrable gastric mucous layer by using secreted HP Trx to reduce the disulfide bonds present in the cysteine-rich mucin regions that are responsible for cross-linking mucin monomers. Therefore, disruption of secreted HP Trx-host protein interaction may result in restoration of the viscoelastic and hydrophobic protective properties of mucus. Previous studies aimed at understanding the nature of cross-reactivity of Trx system components among various species have shown that Trxs have higher affinity for cognate TrxRs (same species), than for TrxRs from different species. However, the basis for this specificity is not known. A growing body of evidence suggests that most protein-protein interactions are mediated by a small number of protein-protein interface residues, referred to as hot spot residues or binding epitopes. Therefore, understanding the biochemical basis of the affinity of proteins for their partners usually begins by identifying the hot spot residues responsible for the protein complex interactions. In this study, the crystal structures of Deinococcus radiodurans thioredoxin reductase (DR TrxR) and Helicobacter pylori TrxR (HP TrxR) were determined at 1.9 Å and 2.4 Å respectively. Analysis of the Trx-binding sites of both structures suggests that the basis of affinity and specificity of Trx for TrxR is primarily due to the shape rather than the charge of the surface. In addition, the complex between Escherichia coli thioredoxin reductase (EC TrxR) and its substrate thioredoxin (EC Trx) was used to identify residues that are responsible for TrxR-Trx interface stability. Using computational alanine scanning mutagenesis and visual inspection of the EC TrxR-Trx interface, 22 EC TrxR side chains were shown to make contact across the TrxR-Trx interface. Although more than 20 EC TrxR side chains make contact across the TrxR-Trx interface, our results suggest that only 4 residues (F81, R130, F141, and F142) account for the majority of the EC TrxR-Trx interface stability. Individual replacement of equivalent DR TrxR residues (M84, K137, F148, F149) with alanine resulted in drastic changes in binding affinity, confirming that the four residues account for most of TrxR-Trx interface stability. These hot spot residues are surrounded by less important residues (hydrophobic and hydrophilic) that are also predicted to contribute to interface stability. F148 and F149 are invariant across bacterial TrxRs, however other residues that contact Trx are less conserved including M84 and K137. When M84 and K137 were changed to match equivalent E. coli TrxR residues (K137R, M84F); D. radiodurans TrxR substrate specificity was altered from its own Trx to that of E. coli Trx. The results suggest that a small subset of the TrxR-Trx interface residues are responsible for the majority of Trx binding affinity and specificity, a property that has been shown to general to protein-protein interfaces.