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Nucleic Acids Research 2003, 31(13):3812–3814. 10.1093/nar/gkg509PubMed CentralView ArticlePubMedGoogle ScholarKumar P, Henikoff S, Ng PC: Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm. The hydrophobic residues provide hydrophobic interactions between the α-helix and the β-sheet. For the simulations of WT and MT ETF:QO, the obtained data demonstrate that after a rapid increase during the first 0.2 ns, the trajectories are stable with average values of 1.43, 1.38 and 1.51 Å for WT and the p.Ala84Thr and p.Phe128Ser ETF:QO mutants, respectively. Statistical analysis of the RMSD data reveals that the trajectories are more stable after the first 1.0 ns. The correlation map for ETF:QO is shown in Figure 5. General structural elements of ETF:QO can be identified by the pattern of the cross-correlations.


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