title: Visualizing the New Zealand Cyber Security Challenge for Attack Behaviors

authors: Garae, Jeffery

subjects: Science & Technology

abstract: Datasets are important for security analytics and mitigation processes in cyber security research and investigations. "Cyber security challenge (CSC)" events provide the means to collect datasets. The New Zealand National cyber security challenge event is designed to promote cyber security education, awareness and equally as important, collect datasets for research purposes. In this paper, we present the: (1) Importance of cyber security challenge events, (2) Highlight the importance of collecting datasets, and (3) present a user-centric security visualization model of attack behaviors. User-centric features with the theoretical concept of Data Provenance as a Security Visualization Service (DPaaSVS) reused to display attacks commencing at the reconnaissance stage through to compromising a defending team machine and exploiting the systems. DPaaSVS creates the ability for users to interact and observe correlations between cyber-attacks. Finally we provide future work on Security Visualization with Augmented Reality capabilities to enhance and improve user interactions with the security visualization platform.

text: Visualizing the New Zealand Cyber Security Challenge for Attack Behaviors Datasets are important for security analytics and mitigation processes in cyber security research and investigations. "Cyber security challenge (CSC)" events provide the means to collect datasets. The New Zealand National cyber security challenge event is designed to promote cyber security education, awareness and equally as important, collect datasets for research purposes. In this paper, we present the: (1) Importance of cyber security challenge events, (2) Highlight the importance of collecting datasets, and (3) present a user-centric security visualization model of attack behaviors. User-centric features with the theoretical concept of Data Provenance as a Security Visualization Service (DPaaSVS) reused to display attacks commencing at the reconnaissance stage through to compromising a defending team machine and exploiting the systems. DPaaSVS creates the ability for users to interact and observe correlations between cyber-attacks. Finally we provide future work on Security Visualization with Augmented Reality capabilities to enhance and improve user interactions with the security visualization platform.

year: 2017

title: Purification and characterization of a thermostable proteinase isolated from Thermus sp. strain Rt41A

authors: Peek, Keith

subjects: enzyme

abstract: Thermus sp. strain Rt41A produces an extracellular thermostable alkaline proteinase. The enzyme has a high isoelectric point (10.25–10.5) which can be exploited in purification by using cation-exchange chromatography. The proteinase was purified to homogeneity and has a molecular mass of 32.5 kDa by SDS/PAGE. It is a glycoprotein, containing 0.7% carbohydrate as glucose equivalents, and has four half-cystine residues present as two disulphide bonds. Maximum proteolytic activity was observed at pH 8.0 against azocasein and greater than 75% of this activity was retained in the pH range 7.0–10.0. Substrate inhibition was observed with casein and azocasein. The enzyme was stable in the pH range 5.0–10.0 and maximum activity, in a 10-min assay, was observed at 90°C with 5 mM CaCl2 present. No loss of activity was observed after 24 h at 70°C and the half-lives at 80°C and 90°C were 13.5 h and 20 min, respectively. Removal of Ca2+ reduced the temperature for maximum proteolytic activity against azocasein to 60°C and the half-life at 70°C was 2.85 min. The enzyme was stable at low and high ionic strength and in the presence of denaturing reagents and organic solvents.
Rt41A proteinase cleaved a number of synthetic amino acid p-nitrophenol esters, the kinetic data indicating that small aliphatic or aromatic amino acids were the preferred residue at the P1 position. The kinetic data for the hydrolysis of a number of peptide p-nitroanilide substrates are also reported. Primary cleavage of the oxidized insulin B chain occurred at sites where the P1′ amino acid was aromatic. Minor cleavage sites (24 h incubation) were for amino acids with aliphatic side chains at the P1′ position. The esterase and insulin cleavage data indicate the specificity is similar for both the P1 and P1′ sites.

text: Purification and characterization of a thermostable proteinase isolated from Thermus sp. strain Rt41A Thermus sp. strain Rt41A produces an extracellular thermostable alkaline proteinase. The enzyme has a high isoelectric point (10.25–10.5) which can be exploited in purification by using cation-exchange chromatography. The proteinase was purified to homogeneity and has a molecular mass of 32.5 kDa by SDS/PAGE. It is a glycoprotein, containing 0.7% carbohydrate as glucose equivalents, and has four half-cystine residues present as two disulphide bonds. Maximum proteolytic activity was observed at pH 8.0 against azocasein and greater than 75% of this activity was retained in the pH range 7.0–10.0. Substrate inhibition was observed with casein and azocasein. The enzyme was stable in the pH range 5.0–10.0 and maximum activity, in a 10-min assay, was observed at 90°C with 5 mM CaCl2 present. No loss of activity was observed after 24 h at 70°C and the half-lives at 80°C and 90°C were 13.5 h and 20 min, respectively. Removal of Ca2+ reduced the temperature for maximum proteolytic activity against azocasein to 60°C and the half-life at 70°C was 2.85 min. The enzyme was stable at low and high ionic strength and in the presence of denaturing reagents and organic solvents.
Rt41A proteinase cleaved a number of synthetic amino acid p-nitrophenol esters, the kinetic data indicating that small aliphatic or aromatic amino acids were the preferred residue at the P1 position. The kinetic data for the hydrolysis of a number of peptide p-nitroanilide substrates are also reported. Primary cleavage of the oxidized insulin B chain occurred at sites where the P1′ amino acid was aromatic. Minor cleavage sites (24 h incubation) were for amino acids with aliphatic side chains at the P1′ position. The esterase and insulin cleavage data indicate the specificity is similar for both the P1 and P1′ sites.

year: 1992

title: Life in a clinical diploma course

authors: Paterson, Keriata

subjects: Maori

abstract: This paper focuses on the author’s experience of a Clinical Diploma programme. The author is a Maori woman who is in her second year of a three year post-graduate Clinical Diploma programme. The paper includes comment on the cultural focus of content, culture conflicts and areas where the programme might be improved for Maori students.

text: Life in a clinical diploma course This paper focuses on the author’s experience of a Clinical Diploma programme. The author is a Maori woman who is in her second year of a three year post-graduate Clinical Diploma programme. The paper includes comment on the cultural focus of content, culture conflicts and areas where the programme might be improved for Maori students.

year: 1993