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Investigating the molecular basis of oligomerisation specificity using coiled coil peptides - Essay Example

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Currently, coiled coils are successfully and extensively used in the designing of multi-stranded structures that are applied in biotechnology, basic research, nanotechnology, and medicine and material science. The broad application range and the critical functions played by…
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Investigating the molecular basis of oligomerisation specificity using coiled coil peptides
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"Investigating the molecular basis of oligomerisation specificity using coiled coil peptides"

Download file to see previous pages The studies have identified that there is unexpected and general correlation between trigger sequences (Indispensable elements for coiled coil formation) and coiled coil oligomerization state specificity .Through the use yeast archytype coiled-coil domain transcriptional factor activator GCN4 as a model system, it was found that oligomerization state determinants that are trimer specific and well established ,switched the topology of the peptide to a trimer from a dimer, only after being inserted into the trigger sequence. The results were confirmed with 2 other coiled coil dimmers that is not related (cortexillin-1 and ATF1).It is further indicated that multiple topology determinants have the capacity of co-existing in the same trigger sequence, and this reveals a delicate balance of the resultant oligomerization state through forces that are position dependent (Steinmetz et al., 2007). Due to the simplicity of this leucine zipper, the alpha helical coiled coil has been traditionally used in a broad number of studies that have targeted the key principles of protein stability, oligomerization and folding (Steinmetz et al., 2007).In this case, the coiled coils currently are exploited as multipurpose tool in various applications seen to be increasing steadily as well as ranging from basic research to medicine.
It is well known that what is referred to as trigger sequence plays a critical role in controlling coiled –coil formation. The distinct feature of several trigger sequences is that they have a capacity of folding into several reasonable stable monomeric helices before the formation of the coiled coil structure (Kammerer et al.1998) Recently, the NMR structures of peptide spanning the GCN4 trigger sequence was solved and indicated that the structure is stabilized by electrostatic interactions and a network of hydrogen bonds (Steinmetz et al., 2007)
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