Significance of Knotted Structures for Function of Proteins and Nucleic Acids - September 17-21, 2014

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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