Fig. 7 | Scientific Reports

Fig. 7

From: A comparative study of computational modeling approaches for evaluating structural dynamics and algorithmic suitability of short length peptides

Fig. 7

Strengths of different algorithms in case of (a). more hydrophobic peptides (b). more hydrophilic peptides. The gmx rms, gmx rmsf, gmx gyrate and gmx sasa functionalities were used to obtain the RMSD, RMSF, Rg and SASA values, respectively. gmx covar and gmx anaeig were used to obtain values for PC1 and PC2. The Gibbs’ free energy values were extracted using gmx-sham. The values were plotted using the OriginPro 2016 64-bit software. The final image inclusive of all the figures alongside the contextual information was designed using Canva (https://www.canva.com/).

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