Abstract
A complete ribosome structure is formed after the 30S and 60S subunits leave the cell nucleus, where all the components of these structures are synthesised. The subunits composed of rRNAs and r-proteins are already constructed in the nucleus. The order of attachment of the r-proteins is already understood. However, the mechanism of the attachment process is not known. The use of a modified fuzzy oil drop model (FOD-M) reveals how hydrophobicity is organised within each protein molecule. This analysis enables an indication of the degree of structural preparation of a given protein for its place within a common structure. The model also assesses the contribution of other, non-aquatic environmental factors to the folding process, which may give rise to speculation about the formation of the 30S unit structure. The 30S structure of the bacterium Thermus thermophilus, available in the Protein Data Bank, which provides data on the composition and three-dimensional structure of this unit, allows the status of the proteins present in the unit to be assessed.
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