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Modified protein was expressed in Escherichia coli Origami (DE3) and was purified.

Covalent functionalization of azide decorated SWNTs with alkyne modified protein was firstly accomplished by the Cu(I -catalyzed [3 + 2] HuI -catalyzedddition.

The binding between PEGylated peptides of various molecular weights and the modified protein was assessed by isothermal calorimetry (ITC), dynamic light scattering (DLS), circular dichroism (CD), and fluorescence anisotropy.

Modified protein was tagged with green fluorescent protein and expressed in B16 melanoma (Fig. 1C).

In all deletions and constructs the proportion of modified protein was clearly lower than that of the full-length USP25m.

To test possible functional consequences, the modified protein was analyzed with two different software packages, PolyPhen [52] and PMut [53].

CKm blots were superimposable with the 3-NT modified 45 kDa band, indicating that the modified protein is CKm.

Nevertheless, the thermal hysteresis activity of the modified protein is indistinguishable from that of native RD3, proving that increased activity of the two-domain antifreeze protein is not dependent on structure of the linker.

As expected, such a modified protein is insensitive to Comm sorting in vitro (from now on it will therefore be referred to as sorting-defective Robo or RoboSD).

Only orthologs with the highest identity to the modified protein were selected from each species.

The lethality (LD50) and phospholipasic activity of native or modified protein were significantly reduced after alkylation (Table 1).