Judul: Perbandingan Oversampling Duplikasi Terhadap Oversampling Acak pada Algoritme K-Nearest Neighbour untuk Kasus Imbalanced Data
Abstrak: Imbalanced class can give negative effect, especially the tendency of the data classes becomes imbalanced. It causes the data will be more inclined to the majority class composition and ignore the minority class. But, minority class sometimes has important information even more difficult to predict than the majority class. In addition, it can also decrease the classifier performance of imbalanced class. The solution will be done by modifying the dataset using duplication oversampling and random oversampling. In this study, a comparison will be made between the random oversampling and duplication oversampling. In this study, we use k-nearest neighbour as the clasifier. The results show that duplication oversampling has better performance than random oversampling, but random oversampling. However, the f-measure of random oversampling is slightly different compared to that of the duplication oversampling
Keyword: Oversampling., K-Nearest Neighbour, Bogor Agricultural University (IPB), Imbalanced data, F-measure

Judul: Klasifikasi Debitur Kartu Kredit Menggunakan Algoritme K-Nearest Neighbor untuk Kasus Imbalanced Data
Abstrak: Data is said to suffer the class imbalanced problem when the class distribution are highly imbalance. In this case, minority class is more difficult to predict then the majority class. Though the minority class sometime has important information. In this paper, classification analysis of credit card debtors is conducted by using k-nearest neighbor that can classify debtors into two categories, good or bad. Analysis of a prospective debtor is essential to minimize credit risk. One approach taken to overcome imbalanced data problems is to modify instance distribution using oversampling and undersampling method. The evaluation is conducted by comparing the value of parameter k, accuracy, precision, recall, and F-measure. The evaluation results show that oversampling technique gives the best result of 96.24% with k = 3, 99.23% recall with k = 2, 95.21% precision with k = 1, and 96.30% F-measure with k = 3.
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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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