One of the active study fields in recent years is the extraction of information from the human face. Numerous investigations on the identification of the most prevalent face variety, including age and gender, have been done. The approach for automatically determining a person's age and gender from their face is suggested in this paper and is based on convolutional neural networks and support vector machines. The four steps of this method are face detection, pre-processing, feature extraction, and classification. A variety of convolutional neural networks have been trained to detect faces in live feed and also determine their age and gender are part of our system. Our model was trained using Adience benchmark dataset for age and gender prediction available on Kaggle, which has produced positive results. Keywords: Convolution neural network, Support Vector Machine, Face Detection, Multi-Task Cascaded Convolution Neural Networks, Principal Component Analysis, Adience benchmark dataset.
ADPGlucose Pyrophosphorylase catalyzes the rate‐limiting step in glucan synthesis. The heat stable T. thermus enzyme is activated by FBP, F6P, and G6P. In order to investigate the molecular basis for heat stability, three unique prolines (P100, 122, 195) have been changed to alanine, and the single and triple mutant proteins purified and characterized. All of the single exhibited reduced Vmax values compared to wild‐type but no significant change in heat stability. The triple mutant had ~30 fold less activity than wild‐type as well as altered apparent affinity for substrates. The wild‐type enzyme was able to utilize CTP, GTP, and UTP in place of ATP to a limited extent, with the alternative nucleotides having Vmax values 15, 3, and 0.1% of wild‐type, respectively. In the presence of UTP, the enzyme displayed higher fold activation. The S0.5 values were increased for these nucleotides as well ranging from a ~20 fold increase for GTP to a 1.5 fold increase for CTP. Molecular modeling indicates involvement of K376 in the allosteric site. In contrast to wild‐type, the K376A enzyme displayed inhibition by the substrate ATP as well as a lower Vmax in the absence of activator. Preliminary data collected at subsaturating ATP concentrations indicates that the altered enzyme has decreased apparent affinity for activators as well as lower fold activation. Supported in part by NSF Grant 0448676.
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