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Abstract

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Objective

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Other Innovations

Crispy Rice Berry Waffle

คณะครุศาสตร์อุตสาหกรรมและเทคโนโลยี

Crispy Rice Berry Waffle

Crispy Rice-berry Snack is a product made from broken rice-berry rice that has been processed into a snack that is thin and crispy, bite-sized. Broken rice-berry rice is cooked, finely ground, and mixed with other ingredients to increase its nutritional value, such as adding plant seeds, adding plant protein nutrients, and then forming it into sheets using heat. The resulting product is a thin sheet, purple-brown in color, crispy, and has the smell of the ingredients used in the production process. It does not contain sugar or sweeteners. It is used as a snack with tea or coffee. Crispy Rice-berry Waffle is a product that contains complete nutrients, including carbohydrates, protein, and fat, which are derived from the ingredients in the production formula.

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Mahachanok mango sauce

คณะอุตสาหกรรมอาหาร

Mahachanok mango sauce

The Mahachanok mango sauce is crafted from low-grade mangoes sourced from Ban Nong Bua Chum in Kalasin Province. Utilizing advanced food science technology, it effectively reduces agricultural waste and enhances product quality. This sauce is enriched with prebiotic fiber that supports the growth of beneficial gut microorganisms. With low sugar content, it is a healthy choice free from artificial colors and flavors. Its rich, natural taste makes it versatile, perfect for enhancing a wide variety of dishes, both savory and sweet.

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Decoding the Impact of RGL3 Genetic Variants on Protein Structure and Binding Site: A Bioinformatics Approach to Uncover Potential Hypertension Associations

คณะแพทยศาสตร์

Decoding the Impact of RGL3 Genetic Variants on Protein Structure and Binding Site: A Bioinformatics Approach to Uncover Potential Hypertension Associations

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.

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