Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation
Protein Sci Goldstein
16: 1887
Supplemental Research Data
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Table S-1: Composition of protein data sets with four different optimal growth temperatures. As with subsequent tables, error estimates represents the variation obtained from bootstrapped datasets.
Table S-2: Values of Esubscriptij (shaded boxes) and Esuperscriptprime subscriptij calculated using the quasi-chemical approximation for four different datasets.
Table S-3: Values of Esubscriptir and Esubscriptrr for the four datasets.
Table S-4: Composition of protein as divided into positively charged (POS, Arg and Lys), negatively charged (NEG, Asp and Glu), aromatic (ARO, Phe, Trp, Tyr), uncharged polar (POL, Asn, Cys, Gln, His, Ser, Thr), and hydrophobic (‘FOB’, Ala, Gly, Ile, Leu, Met, Pro, Val), for the four different datasets.
Table S-5: Values of Esubscriptij (shaded boxes) and Esuperscriptprime subscriptij calculated using the quasi-chemical approximation for four different datasets, grouping residues into categories.
Table S-6: Values of Esubscriptir for the four datasets, grouping residues into categories.
Table S-7: Fraction of the total stabilization energies due to interactions between different residue types, for the different datasets.