Source: http://www.asmscience.org/content/book/10.1128/9781555816827.ch31
Timestamp: 2019-04-21 20:25:58+00:00

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Possible choices of rational design methods for a given level of screening capacity. The upper triangle gives approximate requirements for structural information in the form of percentage of sequence identity (seqid) of the homology model template to the enzyme sequence. The lower triangle specifies the corresponding screening requirements for each approach Npos, number of positrons targeted.
Probability of mutating from a given residue type to another during a single-base change. Random mutations are inherently biased on a residue level, and 42% of all residue-to-residue type changes are impossible. Residues are ordered approximately by hydrophobicity. The figure is read from left to right (row index to column index). Example: the probability of mutating from M to I is higher than mutating from I to M.
A hypothetical energy landscape for an enzyme-catalyzed reaction (black line) compared with the uncatalyzed reaction (gray dotted line). The overall reaction is thermodynamically favorable (ΔGrxn < 0). Notice that, in this case, the catalyzed reaction has only a slightly more favorable activation energy (ΔGcat) than the uncatalyzed reaction (ΔGuncat) due to strong binding to the substrate (ΔGbind). E, ezyme; S, substrate; P, product.
Distribution of mutation effect on the ΔG of protein folding. Data are taken from the Protherm4.0 data set and restricted to single mutations where the protein structure is known ( 8 ). Buried residues are <20% exposed relative to exposure in an alanine-X-alanine tripeptide. Surface residues are defined as having at least 60% relative exposure.
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