Biological
Assembly, Ribosomes and Lambda Phage
We have already dealt with biological assembly in
the folding of polypeptide chains. In that case, although we do not understand
the process well enough to predict how a sequence of amino acids will fold, we
have some of the basic principles well in hand. For most proteins, folding in
the environment of the cell or in physiological buffers appears to be
completely specified by the polypeptide itself. No external folding engine or
scaffolding is required although some of the heat shock proteins assist folding
by binding to proteins in unfolded states and preventing their irreversible
aggregation. Is it also true that large bio-logical structures themselves
contain all the information for their for-mation, or are scaffoldings and
blueprints somehow needed?
Two fundamentally different types of larger
structures are considered in this chapter: the structure and assembly of
ribosomes and the structure and assembly of lambda phage. As we saw, ribosomes
consist of two nonidentical subunits, each containing one or two RNA molecules
and many different ribosomal proteins. The great majority of these proteins are
present in each ribosome as a single copy. Thus, ribosomes are irregular and
asymmetric. On the other hand, lambda phage, and most other viruses, possess a
highly regular coat that covers DNA or RNA molecules. The coat of lambda
consists of many copies of a few proteins that form an icosahedral head in
addition to a number of other proteins that form a tail and tail fibers for
absorption to cells. Both in the case of ribosome assembly and in the case of
virus assembly, one important fundamental problem is determining the as-sembly
order.
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