Judul: Representasi Word Graph Menggunakan XML untuk Kata Benda dalam Bahasa Indonesia
Abstrak: Knowledge graph is one of the methods that can represent semantics of a language. In natural language there are many cases in which the meaning of a sentence is ambiguous. Knowledge graph representation that used in natural language can solve this problem. One of the smallest parts of the knowledge graph is a word graph. Word graph is a graph that represents the meaning of a word. In this study, we represent word graph for Indonesian nouns using eXtensible Markup Language (XML). By using XML, data can be easily interchanged and provide more dynamic data. There were 20 patterns of nominal word graph used in this study. All of the patterns are generated from previous research. Each XML document has a root element which is called graph element. Graph element has two child elements, components and relationships. Components contain all components that form the word graph, and relationships element contain all relation in the word graph. Knowledge graph for Indonesian nouns has been successfully represent in XML. The result of this study is 20 XML documents of Indonesian nouns word graph pattern, and each XML document matching the original pattern in the previous research.
Keyword: Word graph, Indonesian nouns, XML, Knowledge graph

Judul: Representasi Word Graph Menggunakan XML untuk Kata Sifat dalam Bahasa Indonesia
Abstrak: Knowledge Graph (KG) is a method in natural language processing. A part of knowledge graph is known as word graph, a graph which describes the semantic of a word. In this research, we represent word graphs for Indonesian adjectives using eXtensible Markup Language (XML). XML is used to provide facilities in the publication and exchange of data for the next research. Indonesian adjectives in this research are based on the third edition of Kamus Besar Bahasa Indonesia (KBBI). The general pattern in adjective word graph consists of 20 patterns generated from previous research. KG concept has successfully represented in XML forms to facilitate the exchange of data. The result of this research are 21 documents formated in XML forms and the testing result has an accuracy of 100%.
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Judul: Pemurnian dan karakterisasi protein inhibitor RNA helikase virus hepatitis C
Abstrak: Hepatitis C virus (HCV) infection is the second most common chronic viral infection in the world with global prevalence. This infection is contribution to chronic hepatitis and liver cirrhosis, often leading to hepatocellular carcinoma. There is no effective drug and vaccine available against HCV. The current standard treatment, a combination of pegylated interferon-α with ribavirin, is limited by its suboptimal response rate in a significant patient population, side effects, and affordability. Therefore, development of effective drug is needed. One approach to find out the candidate of antiviral drug is to discover the inhibitor of enzyme that essential for virus replication, such as RNA helicase. Streptomyces chartreusis 5-095 produce the inhibitor of HCV RNA helicase. The aim of this study was to purify the protein inhibitor which has inhibition activity against ATPase activity of RNA helicase HCV from S. chartreusis 5-095. The supernatant of culture S. chartreusis 5-095 exhibited high inhibiton activity against ATPase activity of RNA helicase HCV (approximately 72%) at 10 days of incubation. The extracellular protein inhibitor was partially purified by procedures of precipitation with ammonium sulfate to 65% saturation and gel filtration (Sephadex G50) using methanol water solution (4:6) as an eluen. The purity of protein inhibitor was monitored by SDS PAGE. The protein inhibitor showed a relative molecular mass were estimated to be 14 kDa and increased the purity 23,08 fold than those of the crude protein. The specific activity and IC50 after purification were 13,1338 U/mg and 0,0767 mg/mL, respectively. The activity of purified protein inhibitor showed its stability over pH range from 5-8 and optimum at pH 7,4. The inhibition activity showed its stability up to 70% at temperature 100 oC. The purified protein inhibitor relatively stable its activity at storage in the range of -20 oC to room temperature for 35 days.
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