Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.

ABSTRACT: The kinetic folding of ribonuclease H was studied by hydrogen exchange (HX) pulse labeling with analysis by an advanced fragment separation mass spectrometry technology. The results show that folding proceeds through distinct intermediates in a stepwise pathway that sequentially incorporates cooperative native-like structural elements to build the native protein. Each step is seen as a concerted transition of one or more segments from an HX-unprotected to an HX-protected state. Deconvolution of the data to near amino acid resolution shows that each step corresponds to the folding of a secondary structural element of the native protein, termed a "foldon." Each folded segment is retained through subsequent steps of foldon addition, revealing a stepwise buildup of the native structure via a s

SUBMITTER: Hu W 

PROVIDER: S-EPMC3651421 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature