Effects of thermal and electric fields on soybean trypsin inhibitor protein: A molecular modelling study
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- 作者：Brinda Harish Vagadiaa ; brinda.vagadia@mail.mcgill.ca" class="auth_mail" title="E-mail the corresponding author ; Sai Kranthi Vangaa ; Ashutosh Singhb ; Vijaya Raghavana
- 关键词：MD ; molecular dynamics ; SASA ; Solvent Accessible Surface Area ; RMSD ; Root Mean Square Deviation ; STI ; Soybean Trypsin Inhibitor ; KTI ; Kunitz-type Trypsin Inhibitor ; NMR ; Nuclear Magnetic Resonance Imaging ; VMD ; Visual Molecular Dynamics ; FTIR ; Fourier Transformation Infrared Spectroscopy ; PDB ; Protein Data Base ; PME ; Particle Mesh Ewald ; NVT ; ensemble in which number of atoms ; volume and temperature are constant ; NPT ; ensemble in which number of atoms ; pressure and temperature are constant ; DSSP
- 刊名：Innovative Food Science & Emerging Technologies
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：35
- 期：Complete
- 页码：9-20
- 全文大小：3123 K
文摘
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Structural changes in Soybean Trypsin Inhibitor (STI) protein under the external field stress were visualized by Molecular Dynamics (MD) simulation techniques.
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Conformational changes in the STI protein structure were observed using secondary structure analysis (STRIDE) and Root Mean Square Deviation (RMSD) analysis.
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Solvent Accessible Surface Area (SASA) analysis showed visible changes in the secondary structure of the protein.
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Ramachandran plots were used to evaluate the stability of the molecules obtained on treatment with different processing conditions.