Living with Jesus: Practical Christologies in Two Boston American Baptist Churches

This dissertation, an exercise in practical theology, undertakes two tasks. First, it examines how the story of Jesus is appropriated and embodied in the corporate practices of worship and mission (congregational christology) and in the daily lives of ordinary believers (everyday christology) at First Baptist Church in Jamaica Plain and Ruggles Baptist Church in Boston, Massachusetts. Second, it places these practical christologies in dialogue with the academic christology of James McClendon to see what creative and critical insights emerge. A key assumption of the study is that doctrinal reflection is precipitated when the story of Jesus interacts with human stories in both autobiographical and public domains. "Living with Jesus" contends that the understandings of Jesus present in the everyday lives of believers and in a congregation's worship and mission merit the attention of scholars in the disciplines of sociology and theology. This dissertation demonstrates that scholarly research on the visible church, everyday religion, and Christian doctrine pays limited attention to the theologies operative in the everyday lives of believers and congregational practices. A gap exists in scholarly knowledge, which "Living with Jesus" attempts to redress. The empirical results of qualitative research fieldwork are set in the context of historical overviews and contemporary snapshots of First Baptist Church in Jamaica Plain and Ruggles Baptist Church. "Living with Jesus" identifies three types of practical christology operative across the two congregations in corporate practices and the everyday lives of individuals: evangelical christology; exemplarist christology; and prophetic christology. The empirical research shows that for a significant minority of people in the sample, the prevailing understanding of Jesus can best be described as a hybrid christology. By paying attention to McClendon's treatment of the Jesus story and placing the three identified practical christologies in dialogue with his christology, it becomes apparent that each practical christology is simultaneously liberating and limiting. This dissertation argues that evaluating a particular practical christology in relation to the Gospel requires an intentional and disciplined effort on the part of congregations, ordinary believers, and theologians. Questions are proposed to assist further christological reflection on worship, mission, pastoral care, and Christian education.

Visible Volume: a Robust Measure for Protein Structure Characterization

We propose a new characterization of protein structure based on the natural tetrahedral geometry of the β carbon and a new geometric measure of structural similarity, called visible volume. In our model, the side-chains are replaced by an ideal tetrahedron, the orientation of which is fixed with respect to the backbone and corresponds to the preferred rotamer directions. Visible volume is a measure of the non-occluded empty space surrounding each residue position after the side-chains have been removed. It is a robust, parameter-free, locally-computed quantity that accounts for many of the spatial constraints that are of relevance to the corresponding position in the native structure. When computing visible volume, we ignore the nature of both the residue observed at each site and the ones surrounding it. We focus instead on the space that, together, these residues could occupy. By doing so, we are able to quantify a new kind of invariance beyond the apparent variations in protein families, namely, the conservation of the physical space available at structurally equivalent positions for side-chain packing. Corresponding positions in native structures are likely to be of interest in protein structure prediction, protein design, and homology modeling. Visible volume is related to the degree of exposure of a residue position and to the actual rotamers in native proteins. In this article, we discuss the properties of this new measure, namely, its robustness with respect to both crystallographic uncertainties and naturally occurring variations in atomic coordinates, and the remarkable fact that it is essentially independent of the choice of the parameters used in calculating it. We also show how visible volume can be used to align protein structures, to identify structurally equivalent positions that are conserved in a family of proteins, and to single out positions in a protein that are likely to be of biological interest. These properties qualify visible volume as a powerful tool in a variety of applications, from the detailed analysis of protein structure to homology modeling, protein structural alignment, and the definition of better scoring functions for threading purposes.