By Patricia M. Dove, James J. De Yoreo, Steve Weiner
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Additional resources for Biomineralization
Leadbeater BSC, Riding R (eds) Oxford University Press, New York, p 1-17 Lowenstam HA, Margulis L (1980) Calcium regulation and the appearance of calcareous skeletons in the fossil record. In: The Mechanisms of Biomineralization in Animals and Plants. Omori M, Watabe N (eds) Tokai University Press, Tokyo, p 289-300 Lowenstam HA, Rossman GR (1975) Amorphous, hydrous, ferric phosphatic dermal granules in Molpadia (Holothurodidea): Physical and chemical characterization and ecologic implications of the bioinorganic fraction.
Figure 4. Overview of protein translation. The scheme for building the polypeptide chain using the codons provided by mRNA starts with the assembly of the small and large ribosomal subunits at the mRNA AUG initiation codon to form the ribosomal complex. This assembly takes place at the AUG initiation codon of the mRNA, and requires the aminoacyl tRNA-Met and proteins called initiation factors to allow ribosomal assembly to proceed. Next, with the help of elongation factor proteins, the aminoacyl tRNA which has an anticodon that matches the next mRNA codon enters the “A” site of the ribosome.
In globular proteins which adopt a compact, folded structure in solution, there are several categories of secondary structure: for example, α−helix (Fig. 5), β−sheet, 310 helix, β−helix, β−turn, polyproline type II. These structures, in turn, can be organized into supersecondary structures, which are clusters of individual secondary structure units. For example, two contiguous α−helices that are clustered together are referred to as coiled coils; two β−strands which possess an intervening α−helix are referred to as “βαβ” unit, and so on.