Expanding from a public park design project to a campus design on an area of over 50 rai in Ang Sila Subdistrict, Mueang District, Chonburi Province, to serve as both an educational institution and a place for relaxation and learning for the surrounding people.
การพัฒนาพื้นที่แห่งนี้ให้กลายเป็นCampus Park เพื่อเป็นพื้นที่พักผ่อนและแลกเปลี่ยนความรู้เกี่ยวกับระบบนิเวศชายหาดของจังหวัดชลบุรี
คณะเทคโนโลยีสารสนเทศ
This thesis aims to present the development of a metaverse project for the KMITL Lifelong Learning Center (KLLC) and KMITL Data Management Center (KDMC) for Public Relations at King Mongkut's Institute of Technology Ladkrabang, with the main goal of creating a metaverse prototype to promote learning and public relations through virtual reality technology for students, staff, and external individuals. In this project, the developers have created a metaverse system to simulate a virtual experience for users at the KMITL Lifelong Learning Center (KLLC) and KMITL Data Management Center (KDMC) for Public Relations at King Mongkut's Institute of Technology Ladkrabang. Users will be able to access the system through a web application developed with Unity, which is the tool used to create the metaverse system. The design allows users to visit and interact with various locations within the building to promote public relations in a more widespread virtual format. The developers used Maya and Unity software to create a metaverse system for modeling 3D objects and managing various functions, providing users with a realistic and novel experience. This project is expected to promote learning and the dissemination of information in an easily accessible modern format, creating opportunities for education and learning for those who cannot travel to see the actual locations. This makes metaverse technology an important tool for effectively developing learning and engagement in the digital age.
คณะวิศวกรรมศาสตร์
ยานยนต์ไฟฟ้าดัดแปลง
คณะแพทยศาสตร์
Background: The RGL3 gene plays a role in key signal transduction pathways and has been implicated in hypertension risk through the identification of a copy number variant deletion in exon 6. Genome-wide association studies have highlighted RGL3 as associated with hypertension, providing insights into the genetic underpinnings of the condition and its protective effects on cardiovascular health. Despite these findings, there is a lack of data that confirms the precise role of RGL3 in hypertension. Additionally, the functional impact of certain variants, particularly those classified as variants of uncertain significance, remains poorly understood. Objectives: This study aims to analyze alterations in the RGL3 protein structure caused by mutations and validate the location of the ligand binding sites. Methods: Clinical variants of the RGL3 gene were obtained from NCBI ClinVar. Variants of uncertain significance and likely benign were analyzed. Multiple sequence alignment was conducted using BioEdit v7.7.1. AlphaFold 2 predicted the wild-type and mutant 3D structures, followed by quality assessment via PROCHECK. Functional domain analysis of RasGEF, RASGEF_NTER, and RA domains was performed, and BIOVIA Discovery Studio Visualizer 2024 was used to evaluate structural and physicochemical changes. Results: The analysis of 81 RGL3 variants identified 5 likely benign and 76 variants of uncertain significance (VUS), all of which were missense mutations. Structural modeling using AlphaFold 2 revealed three key domains: RasGEF_NTER, RasGEF, and RA, where mutations induced conformational changes. Ramachandran plot validation confirmed 79.7% of residues in favored regions, indicating an overall reliable structure. Moreover, mutations within RasGEF and RA domains altered polarity, charge, and stability, suggesting potential functional disruptions. These findings provide insight into the structural consequences of RGL3 mutations, contributing to further functional assessments. Discussion & Conclusion: The identified RGL3 mutations induced physicochemical alterations in key domains, affecting charge, polarity, hydrophobicity, and flexibility. These changes likely disrupt interactions with Ras-like GTPases, impairing GDP-GTP exchange and cellular signaling. Structural analysis highlighted mutations in RasGEF and RA domains that may interfere with activation states, potentially affecting protein function and stability. These findings suggest that mutations in RGL3 could have functional consequences, emphasizing the need for further molecular and functional studies to explore their pathogenic potential.