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 PT-values) are fairly constant for the five PDZ domains. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
A conserved folding mechanism for PDZ domains / Celestine N., Chi; Gianni, Stefano; Calosci, Nicoletta; TRAVAGLINI ALLOCATELLI, Carlo; K., Engstrom; Per, Jemth. - In: FEBS LETTERS. - ISSN 0014-5793. - 581:6(2007), pp. 1109-1113. [10.1016/j.febslet.2007.02.011]
A conserved folding mechanism for PDZ domains
GIANNI, STEFANO;CALOSCI, NICOLETTA;TRAVAGLINI ALLOCATELLI, Carlo;
2007
Abstract
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 PT-values) are fairly constant for the five PDZ domains. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
