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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Tailoring the properties of (catalytically)-active inclusion bodies

Fig. 6

Computational analysis of the a, b sequence-based and c structural determinants of CatIB/FIB formation analyzed based on the TDoT dataset. a Sequence-based aggregation propensities were inferred using the AGGRESCAN webserver [72] and the average aggregation-propensity values per amino acid (a4v) normalized to a 100-residue protein (Na4vSS) were used as indicator for aggregation. Low (negative) Na4vSS are an indicator for low aggregation propensity as for example demonstrated for intrinsically disordered proteins (IDPs) [72]. b The relative change of the Na4vSS value due to addition of the TDoT domain \(\left( {{\Delta Na}^{4} \text{vSS} = \left( {\frac{{\left( {\text{Na}^{4} \text{vSS}_{{\text{fusion}}} - \varvec{ }\text{Na}^{4} \text{vSS}_{{\text{target}}} } \right)}}{{\left| {\text{Na}^{4} \text{vSS}_{{\text{target}}} } \right|}}} \right) \times 100} \right)\) has in the past been used for the computation of the effects of point mutations on aggregation [72]. Positive values suggest increased and negative values decreased aggregation due to addition of the TDoT domain. c The presence/absence of large hydrophobic surface patches for the corresponding target protein structures was quantified using the hpatch tool implemented in Rosetta [75, 76, 94]. Surface areas were quantified using Pymol 1.7.0.0 (Schrödinger, LCC, New York, NY, USA). In a and c CatIB-formation was plotted as the relative activity in the insoluble fraction (Additional file 1: Table S1). Coefficient of determination (R2) values are always given excluding the blue-highlighted outliers (black) and including the outliers (blue)

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