Significance of Knotted Structures for Function of Proteins and Nucleic Acids
Opening Session
Unfolded, but Not Knotted! Mechanistic Studies of IDP Folding upon Binding
Jane Clarke
.
University of Cambridge, Cambridge, United Kingdom.
Many intrinsically disordered proteins function by folding upon binding to a target protein. It is
often said that IDPs provide high specificity with low affinity, but kinetic analysis of a number
of systems suggests that this is not universally correct. Why then are disordered proteins so
ubiquitous? Is disorder in the IDP important for the function? I will discuss some of our recent
kinetic and mechanistic studies of a number of IDPs that fold upon binding.
Ribosomes: RNA Machines for Protein Production that Withstand Evolution Pressures
Ada Yonath.
Department of Structural Biology, Weizmann Institute, Rehovot, Israel.
Ribosomes, the universal cellular machines for translation of the genetic code into proteins,
possess spectacular architecture accompanied by inherent mobility, allowing for their smooth
performance as polymerases that translate the genetic code into proteins. The site for peptide
bond formation is located within a universal internal semi-symmetrical region. The high
conservation of this region implies its existence irrespective of environmental conditions and
indicates that it may represent an ancient RNA machine. Hence, it could be the kernel around
which life originated. The mechanistic and genetic applications of this finding will be discussed.
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