Abstract
Although we have a rather elaborate 'working-cycle' for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage-type chaperones to emphasize that they provide a closed, protected environment to help the folding of their substrates, our understanding of the molecular mechanism of how these chaperones help protein folding is still incomplete. The present study adds two novel elements to the mechanism of how Anfinsen-cage-type chaperones (members of the 60 kDa chaperone family) aid protein folding. It is proposed that (1) these chaperones do not generally unfold their targets, but by a multidirectional expansion preferentially loosen the tight, inner structure of the collapsed target protein', and (2) during the expansion water molecules enter the hydrophobic core of the target, this percolation being a key step in chaperone action. This study compares this chaperone-percolator model with existing explanations and suggests further experiments to test it.
| Original language | English |
|---|---|
| Pages (from-to) | 959-965 |
| Number of pages | 7 |
| Journal | BioEssays |
| Volume | 21 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 1999 |
Fingerprint
ASJC Scopus subject areas
- Neuroscience (miscellaneous)
- Biochemistry
- Cell Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Developmental Biology
- Agricultural and Biological Sciences (miscellaneous)
- Plant Science
Cite this
Chaperone-percolator model : A possible molecular mechanism of anfinsen-cage-type chaperones. / Csermely, P.
In: BioEssays, Vol. 21, No. 11, 11.1999, p. 959-965.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Chaperone-percolator model
T2 - A possible molecular mechanism of anfinsen-cage-type chaperones
AU - Csermely, P.
PY - 1999/11
Y1 - 1999/11
N2 - Although we have a rather elaborate 'working-cycle' for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage-type chaperones to emphasize that they provide a closed, protected environment to help the folding of their substrates, our understanding of the molecular mechanism of how these chaperones help protein folding is still incomplete. The present study adds two novel elements to the mechanism of how Anfinsen-cage-type chaperones (members of the 60 kDa chaperone family) aid protein folding. It is proposed that (1) these chaperones do not generally unfold their targets, but by a multidirectional expansion preferentially loosen the tight, inner structure of the collapsed target protein', and (2) during the expansion water molecules enter the hydrophobic core of the target, this percolation being a key step in chaperone action. This study compares this chaperone-percolator model with existing explanations and suggests further experiments to test it.
AB - Although we have a rather elaborate 'working-cycle' for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage-type chaperones to emphasize that they provide a closed, protected environment to help the folding of their substrates, our understanding of the molecular mechanism of how these chaperones help protein folding is still incomplete. The present study adds two novel elements to the mechanism of how Anfinsen-cage-type chaperones (members of the 60 kDa chaperone family) aid protein folding. It is proposed that (1) these chaperones do not generally unfold their targets, but by a multidirectional expansion preferentially loosen the tight, inner structure of the collapsed target protein', and (2) during the expansion water molecules enter the hydrophobic core of the target, this percolation being a key step in chaperone action. This study compares this chaperone-percolator model with existing explanations and suggests further experiments to test it.
UR - http://www.scopus.com/inward/record.url?scp=0033231417&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033231417&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1521-1878(199911)21:11<959::AID-BIES8>3.0.CO;2-1
DO - 10.1002/(SICI)1521-1878(199911)21:11<959::AID-BIES8>3.0.CO;2-1
M3 - Article
VL - 21
SP - 959
EP - 965
JO - BioEssays
JF - BioEssays
SN - 0265-9247
IS - 11
ER -