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This study investigates the implementation process of a Continuous Improvement (CIm) tool using the strategy-as-practice (s-as-p) perspective. The research is underpinned by the theoretical approaches of innovation process research, CIm theory and the s-as-p perspective. There are a limited number of empirical studies actually describing the implementation process of CIm tools. In identifying the need to study the behavioural aspects of CIm implementation, this study evaluated the use of a tool as something that people “do” rather than something that organisations “have”. By adopting the s-as-p theoretical approach it addressed strategy as a phenomenon consisting of social action. The scope of the research strategy was to explore the implementation process and to gain a thorough understanding of this. Therefore, a multi-focus case study research strategy was adopted comparing and contrasting, through rich qualitative analysis, eight cases that were either new to or had had experience in using a CIm tool. The research concluded that “collective practice” significantly influences the internal life of the implementation process, which is not guided by linear activities but by a process of improvisation that requires company-wide commitment. It was evident that the factors facilitating the implementation process were a set of incrementally and culturally acquired practices such as leadership functions and the collective practices of the wider workforce. Implementation process barriers were associated with low staff engagement, industry problems, knowledge and strategy-related factors. The implementation appeared to have enhanced the capability of the participant organisations to continuously improve and to exploit knowledge. The findings make some important contributions to the s-as-p perspective and to the literature on CIm by illustrating how CIm is practiced and integrated within firms through the use of a standards-driven tool; the study illustrates that CIm is not something that organisations have through CIm tools but is something that organisations should constantly be reaching through collective practices. Finally, the research suggests that the specific characteristics of the hospitality industry may influence some of the CIm behaviours and therefore demonstrates that any strategy implementation requires research contextually relevant to the industry.

Chaperone proteins and their cochaperones are perhaps one of the most intriguing systems for investigation. Ubiquitous in nature, they can be found in every organism and that perhaps is the reason that their sequence shows amazingly high homology and similarity. Allosteric mechanisms govern their functions and that makes them very interesting and hard to investigate at the same time. In medicine, chaperone proteins are of extreme interest since they are related to various diseases including neurodegerative diseases such as Alzheimers disease, Pick’s disease and Parkinsons disease. Various forms of cancer also relate to the chaperone proteins. Hence the investigation of various small molecules that could up/down-regulate this system is of great biomedical relevance. In this dissertation we explored a member of the chaperone family that is constitutively expressed in every mammalian cell, the cognate Hsp70 (Hsc70). More specifically, we investigate the interactions of its ATPase domain with various small molecules that either act as inhibitors or enhancers of the protein’s activity. For example, we found that the compound MKT-077 blocks the Hsc70 ATPase activity by binding in a negatively charged cleft with its positive charge. This was identified with the use of chemical shift mapping experiments, NOE experiments and AUTODOCK simulations. MKT-077 binds only to the ADP form of the protein elucidating an amazing mechanism for the inhibition of the protein. Another inhibitor, methylene blue, binds to another locus of the ATPase. Interestingly, both of these molecules reduce the levels of tau in cell-based models of Alzheimers disease. This would suggest that the use of compounds that bind to Hsc70 at two separate sites could modulate Hsp70 activity in cells in a synergistic fashion.