
pmid: 16751091
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.
Models, Molecular, Molecular Weight, Protein Folding, Bacteria, Biochemistry, Genetics and Molecular Biology(all), Protein Conformation, Amino Acid Motifs, Amino Acid Sequence, Chaperonin 60
Models, Molecular, Molecular Weight, Protein Folding, Bacteria, Biochemistry, Genetics and Molecular Biology(all), Protein Conformation, Amino Acid Motifs, Amino Acid Sequence, Chaperonin 60
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 42 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
