Direct observation of chaperone-induced changes in a protein folding pathway.

@article{citeulike:2149252, abstract = {How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped. Interactions with SecB completely prevent stable tertiary contacts in the core structure but have no detectable effect on the folding of the external alpha helices. It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions.}, address = {Department of Molecular Microbiology, Groningen Bio-molecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands.}, author = {Bechtluft, P. and van Leeuwen, R. G. and Tyreman, M. and Tomkiewicz, D. and Nouwen, N. and Tepper, H. L. and Driessen, A. J. and Tans, S. J. }, citeulike-article-id = {2149252}, doi = {10.1126/science.1144972}, issn = {1095-9203}, journal = {Science}, keywords = {chaperone, folding}, month = {November}, number = {5855}, pages = {1458--1461}, posted-at = {2008-01-15 05:59:52}, priority = {2}, title = {Direct observation of chaperone-induced changes in a protein folding pathway.}, url = {http://dx.doi.org/10.1126/science.1144972}, volume = {318}, year = {2007} }

TY - JOUR ID - citeulike:2149252 L3 - citeulike-article-id:2149252 TI - Direct observation of chaperone-induced changes in a protein folding pathway. JF - Science VL - 318 IS - 5855 SP - 1458 EP - 1461 AD - Department of Molecular Microbiology, Groningen Bio-molecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands. SN - 1095-9203 N2 - How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped. Interactions with SecB completely prevent stable tertiary contacts in the core structure but have no detectable effect on the folding of the external alpha helices. It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions. KW - chaperone KW - folding AU - Bechtluft, P AU - van Leeuwen, RG AU - Tyreman, M AU - Tomkiewicz, D AU - Nouwen, N AU - Tepper, HL AU - Driessen, AJ AU - Tans, SJ PY - 2007/11/30/ UR - http://dx.doi.org/10.1126/science.1144972 ER -