A conserved folding mechanism for PDZ domains
2007 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 581, no 6, 1109-1113 p.Article in journal (Refereed) Published
An important question in protein folding is whether the folding mechanism is sequence dependent and conserved for homologous proteins. In this work we compared the kinetic folding mechanism of five postsynaptic density protein-95, disc-large tumor suppressor protein, zonula occludens-1 (PDZ) domains, sharing similar topology but having different primary structures. Investigation of the different proteins under various experimental conditions revealed that the folding kinetics of each member of the PDZ family can be described by a model with two transition states separated by an intermediate. Moreover, the positions of the two transition states along the reaction coordinate (as given by their βT-values) are fairly constant for the five PDZ domains.
Place, publisher, year, edition, pages
2007. Vol. 581, no 6, 1109-1113 p.
Folding mechanism, Kinetics, PDZ domain, Protein folding
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-15771DOI: 10.1016/j.febslet.2007.02.011ISI: 000245370600006PubMedID: 17316619OAI: oai:DiVA.org:uu-15771DiVA: diva2:43542