Majestic Gamification:a case study in the adoption of a service innovation

Purpose: A case study is presented concerning a gamified awards system designed to encourage software users to explore a suite of tools, and to share their expertise level in profile pages. Majestic is a high-tech business based in the West Midlands (UK) w hich offers a Link Intelligence database using a Software as a Service (SaaS) business model. Customers leverage the database for tasks including Search Engine Optimisation (SEO) by using a suite of web-based tools. Getting to know all the tools and how they can be deployed to good effect represents a considerable learning challenge, and Majestic were aware that. Design/methodology/approach: We present the development of Majestic Awards as a case study highlighting the most important design decisions. Then we reflect on the development process as an example of innovation adoption, thereby identifying resources and cu ltura l factors which were critical in ensuring the success of the project. Findings: The gamified awards system makes learning the tools an enjoyable, explorative experience. Success factors included identifying a clear business goal, the process/ project f it, senior management buy in, and identifying the knowledge and resources to resolve t echnical issues. Originality/value: Prior to gamification of the system, only the most expert users regu larly utilized all the tools. The user base is now more knowl edgable about the system and some users choose to use the system to publicize their expertise.

Peptide binding to HLA-DP proteins at pH 5.0 and pH 7.0:a quantitative molecular docking study

Background: HLA-DPs are class II MHC proteins mediating immune responses to many diseases. Peptides bind MHC class II proteins in the acidic environment within endosomes. Acidic pH markedly elevates association rate constants but dissociation rates are almost unchanged in the pH range 5.0 - 7.0. This pH-driven effect can be explained by the protonation/deprotonation states of Histidine, whose imidazole has a pKa of 6.0. At pH 5.0, imidazole ring is protonated, making Histidine positively charged and very hydrophilic, while at pH 7.0 imidazole is unprotonated, making Histidine less hydrophilic. We develop here a method to predict peptide binding to the four most frequent HLA-DP proteins: DP1, DP41, DP42 and DP5, using a molecular docking protocol. Dockings to virtual combinatorial peptide libraries were performed at pH 5.0 and pH 7.0. Results: The X-ray structure of the peptide - HLA-DP2 protein complex was used as a starting template to model by homology the structure of the four DP proteins. The resulting models were used to produce virtual combinatorial peptide libraries constructed using the single amino acid substitution (SAAS) principle. Peptides were docked into the DP binding site using AutoDock at pH 5.0 and pH 7.0. The resulting scores were normalized and used to generate Docking Score-based Quantitative Matrices (DS-QMs). The predictive ability of these QMs was tested using an external test set of 484 known DP binders. They were also compared to existing servers for DP binding prediction. The models derived at pH 5.0 predict better than those derived at pH 7.0 and showed significantly improved predictions for three of the four DP proteins, when compared to the existing servers. They are able to recognize 50% of the known binders in the top 5% of predicted peptides. Conclusions: The higher predictive ability of DS-QMs derived at pH 5.0 may be rationalised by the additional hydrogen bond formed between the backbone carbonyl oxygen belonging to the peptide position before p1 (p-1) and the protonated ε-nitrogen of His 79β. Additionally, protonated His residues are well accepted at most of the peptide binding core positions which is in a good agreement with the overall negatively charged peptide binding site of most MHC proteins. © 2012 Patronov et al.; licensee BioMed Central Ltd.