| Literature DB >> 16751091 |
Abstract
The chaperonin GroEL has been thought of as an important but passive player in protein folding, providing an encapsulated environment that allows folding to proceed unimpaired by aggregation. In this issue, Tang et al. (2006) redesign the GroEL central cavity and show that the chaperonin cage can alter the rate of folding and, for some proteins, could even alter the folding mechanism.Entities:
Mesh：
Substances：
Year: 2006 PMID： 16751091 DOI： 10.1016/j.cell.2006.05.021
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582