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News and Views
Nature 431, 520-522 (30 September 2004) | doi:10.1038/431520a; Published online 29 September 2004
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Faculty Position in Mathematical Biology
- The Ohio State University
- Ohio, USA
Research Fellow in Bone-ligamentous Tissue Scaffolds
- University of Leeds
- Leeds, UK
Cell biology: Sight at the end of the tunnel
Arthur Horwich1
Abstract
A chaperone molecule called trigger factor binds new polypeptide chains as they emerge from the protein-synthesis machinery. Crystal structures suggest that this molecule forms a hydrophobic 'cradle'.
Cells seem to leave nothing to chance, including the final step of information transfer — the folding of a newly made chain of amino acids into a three-dimensional, active, 'native' protein. Specialized proteins called molecular chaperones ensure that the process of folding, determined by the amino-acid sequence of a polypeptide chain, does not go awry1, 2.
- Arthur Horwich is in the Department of Genetics and the Howard Hughes Medical Institute, Boyer Center, Yale School of Medicine, New Haven, Connecticut 06510, USA, and The Scripps Research Institute, La Jolla, California, USA.
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