Sandbox20: Difference between revisions
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[[Image:Hydrophobic residues in RTP.jpg | thumb | upright=1.5| right| Hydrophobic surfaces within each RTP monomer support their conformation.]] | [[Image:Hydrophobic residues in RTP.jpg | thumb | upright=1.5| right| Hydrophobic surfaces within each RTP monomer support their conformation.]] | ||
The association of α4 helices into an antiparellel coiled coil leads to dimerisation (left). The conformation is further stabilised by interhelical salt bridges outside this region, as well as an aromatic network on the inner surface which form a hydrophobic core | The association of α4 helices into an antiparellel coiled coil leads to dimerisation (left). The conformation is further stabilised by interhelical salt bridges outside this region, as well as an aromatic network on the inner surface which form a hydrophobic core. The phenylalanine and tryptophan residues that form part of this network are shown in the image (right). | ||
The crystal structure of [[1bm9| RTP in its unbound state]] was determined in 1995. A [[1j0r| C110S mutant]] was then generated to prevent the aggregation of RTP through cysteine oxidation. With a very similar structure and almost no change in dimerisation and DNA-binding capacities, the mutant was the protein of choice for later studies. | The crystal structure of [[1bm9| RTP in its unbound state]] was determined in 1995. A [[1j0r| C110S mutant]] was then generated to prevent the aggregation of RTP through cysteine oxidation. With a very similar structure and almost no change in dimerisation and DNA-binding capacities, the mutant was the protein of choice for later studies. | ||