Rethinking Validity in Qualitative Research from a Social Constructionist Perspective: From Is this Valid Research? To What Is this Research Valid for?

This article theorizes the issue of validity that is premised upon social constructionist assumptions, particularly as it is applied to the assessment of qualitative research. As a social construction, validity must thus be interrogated for its discursive function within the social sciences. I will argue that, as a criterion of assessment, validity polices the social science enterprise and thus, functions as a practice of power through the de/legitimation of social knowledge, research practice, and experiential possibilities. This critique will lead into a reformulation of validity that actively recognizes and negotiates its practice of power. Within this reformulation, research findings are conceptualized as representations and should be scrutinized for their realist, critical, deconstructive, and reflexive narrative function. Put simply, assessing qualitative research entails multiple and contradictory readings of its representational failures and successes. Therefore, validity is no longer conceived as a determination (i.e., is valid versus is not valid) but a continual process of interrogation. This new framework will be applied to my Masters thesis research that explored domestic violence and relationship abuse among gay males. Implications for research practice are discussed

Structural evolution of C-terminal domains in the p53 family

The tetrameric state of p53, p63, and p73 has been considered one of the hallmarks of this protein family. While the DNA binding domain (DBD) is highly conserved among vertebrates and invertebrates, sequences C-terminal to the DBD are highly divergent. In particular, the oligomerization domain (OD) of the p53 forms of the model organisms Caenorhabditis elegans and Drosophila cannot be identified by sequence analysis. Here, we present the solution structures of their ODs and show that they both differ significantly from each other as well as from human p53. CEP-1 contains a composite domain of an OD and a sterile alpha motif (SAM) domain, and forms dimers instead of tetramers. The Dmp53 structure is characterized by an additional N-terminal β-strand and a C-terminal helix. Truncation analysis in both domains reveals that the additional structural elements are necessary to stabilize the structure of the OD, suggesting a new function for the SAM domain. Furthermore, these structures show a potential path of evolution from an ancestral dimeric form over a tetrameric form, with additional stabilization elements, to the tetramerization domain of mammalian p53