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Updated: Jul 15, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Thermal titration molecular dynamics (TTMD) reveals the temperature-dependent structural stability of major royal
Yelin Adalina1, Gusnia Meilin Gholam2, Dimas Andrianto3
1Research Center for Applied Botany, National Research and Innovation Agency (BRIN), Cibinong, Bogor, 16911, Indonesia.
Abstract:
Major royal jelly protein 1 (MRJP1) is recognized as the principal component of royal jelly (RJ); therefore, investigating its optimal structural behavior under different environmental temperature conditions may provide insight into appropriate storage strategies for RJ. In this study, a thermal titration molecular dynamics (TTMD) approach was employed using a 100 ns simulation trajectory, followed by a comprehensive evaluation that included RMSD, RMSF, radius of gyration (Rg), secondary structure analysis, principal component analysis (PCA), normal mode analysis (NMA), free energy landscape (FEL), residue interaction network (RIN), and residue communication pattern analysis under a series of temperature conditions (277 K, 300 K, 310 K, 320 K, 329 K, 338 K, and 369 K). MRJP1 is predicted to undergo a series of conformational transitions, alterations in residue communication patterns, and stability changes in response to temperature variations. Overall, the analysis indicated that a temperature range of 277-310 K may represent a favorable stability window for MRJP1. Nevertheless, experimental validation under laboratory conditions is required to confirm the predictions obtained from this computational study.
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