Development and benchmark to obtain AMBER parameters dataset for non-standard amino acids modified with 4-hydroxy-2-nonenal

The data described here support the research article “4-HNE carbonylation induces local conformational changes on bovine serum albumin and thioredoxin. A molecular dynamics study” (Alviz-Amador et al., 2018) . Dataset on Gaff force field parameters of AMBER is provided for assembled three non-standa...

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Bibliographic Details
Published in:Data in brief 2018-12, Vol.21, p.2581-2589
Main Authors: Alviz-Amador, Antistio, Galindo-Murillo, Rodrigo, Pineda-Alemán, Rafael, Pérez-González, Humberto, Rodríguez-Cavallo, Erika, Vivas-Reyes, Ricardo, Méndez-Cuadro, Darío
Format: Article
Language:English
Subjects:
AMBER
Biochemistry, Genetics and Molecular Biology
Force field parameterization
Gaff
Geometry optimization
Mechanical quantic
Molecular dynamics
Validation
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Summary:The data described here support the research article “4-HNE carbonylation induces local conformational changes on bovine serum albumin and thioredoxin. A molecular dynamics study” (Alviz-Amador et al., 2018) . Dataset on Gaff force field parameters of AMBER is provided for assembled three non-standard amino acids resulting of the 4-HNE Michael addition, the main end product of lipids peroxidation. Data include a framework for derivation of missing bonds, angles and dihedral parameters for Cys, His, and Lys modified amino acids, alongside optimized partial charges derived with Restrained Electrostatic Potential (RESP) method and the new force field parameters obtained by quantic mechanical (QM) using HF/6-31G** level of theory. Benchmark as a graphics tutorial summary steps to obtained new parameters and the validation of non-standard amino acids is presented. The new residues constructed are put available to the scientific community to perform molecular dynamics simulations of modified 4-HNE proteins.
ISSN:2352-3409
2352-3409
DOI:10.1016/j.dib.2018.11.102