The energy landscape of modular repeat proteins: topology determines folding mechanism in the ankyrin family. Export

@article{citeulike:406768, abstract = {Proteins consisting of repeating amino acid motifs are abundant in all kingdoms of life, especially in higher eukaryotes. Repeat-containing proteins self-organize into elongated non-globular structures. Do the same general underlying principles that dictate the folding of globular domains apply also to these extended topologies? Using a simplified structure-based model capturing a perfectly funneled energy landscape, we surveyed the predicted mechanism of folding for ankyrin repeat containing proteins. The ankyrin family is one of the most extensively studied classes of non-globular folds. The model based only on native contacts reproduces most of the experimental observations on the folding of these proteins, including a folding mechanism that is reminiscent of a nucleation propagation growth. The confluence of simulation and experimental results suggests that the folding of non-globular proteins is accurately described by a funneled energy landscape, in which topology plays a determinant role in the folding mechanism.}, address = {Center for Theoretical Biological Physics, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA; Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.}, author = {Ferreiro, D. U. and Cho, S. S. and Komives, E. A. and Wolynes, P. G.}, citeulike-article-id = {406768}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jmb.2005.09.078}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16257414}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16257414}, day = {2}, doi = {10.1016/j.jmb.2005.09.078}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {ankyrin-repeats, folding}, month = {December}, number = {3}, pages = {679--692}, posted-at = {2005-11-24 02:06:26}, priority = {2}, title = {The energy landscape of modular repeat proteins: topology determines folding mechanism in the ankyrin family.}, url = {http://dx.doi.org/10.1016/j.jmb.2005.09.078}, volume = {354}, year = {2005} }

TY - JOUR ID - citeulike:406768 L3 - citeulike-article-id:406768 N2 - Proteins consisting of repeating amino acid motifs are abundant in all kingdoms of life, especially in higher eukaryotes. Repeat-containing proteins self-organize into elongated non-globular structures. Do the same general underlying principles that dictate the folding of globular domains apply also to these extended topologies? Using a simplified structure-based model capturing a perfectly funneled energy landscape, we surveyed the predicted mechanism of folding for ankyrin repeat containing proteins. The ankyrin family is one of the most extensively studied classes of non-globular folds. The model based only on native contacts reproduces most of the experimental observations on the folding of these proteins, including a folding mechanism that is reminiscent of a nucleation propagation growth. The confluence of simulation and experimental results suggests that the folding of non-globular proteins is accurately described by a funneled energy landscape, in which topology plays a determinant role in the folding mechanism. IS - 3 JF - J Mol Biol SN - 0022-2836 AD - Center for Theoretical Biological Physics, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA; Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. EP - 692 TI - The energy landscape of modular repeat proteins: topology determines folding mechanism in the ankyrin family. VL - 354 SP - 679 KW - ankyrin-repeats KW - folding AU - Ferreiro, DU AU - Cho, SS AU - Komives, EA AU - Wolynes, PG PY - 2005/12/02/ UR - http://dx.doi.org/10.1016/j.jmb.2005.09.078 ER -