Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase
Protein Sci Sibille et al.
15: 1915
Supplemental Research Data
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Fig. S1 shows the backbone positional RMSD from the starting crystal structure and electrostatic
and van der Waals energies as a function of the MD simulation time.
Fig. S2 shows the B-factors as a function of the residue sequence as calculated from the last 10 ns
of the MD simulation of the wild type (WT) and PG mutant lipase.
Table S1 reports the calculated spectral density values for WT lipase.
Table S2 reports the calculated spectral density values for PG lipase
Table S3 reports the slowing factor {log(kc/kex} calculated from H-D exchange deuterium data for both PG and Wt type proteins.
