Volume 9 Issue 6, June 2002

A new study has demonstrated that the E. coli Hsp70, DnaK, can catalyze cis-trans isomerization of non-prolyl peptide bonds.

A new 20-residue peptide represents the smallest example to date of cooperatively folded tertiary structure. This achievement provides a new tool for elucidating protein conformational preferences. The mini-protein should serve as a fruitful platform for protein design.

Housekeeping is not a humdrum process when it comes to protein quality control. Inside chaperone-protease machines, proteins are subject to dramatic life or death trials and must shape up rapidly to survive. Accumulation of aberrantly folded proteins is the basis of many diseases, so the outcome is vitally important to the cell.