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A conserved folding mechanism for PDZ domains
Author(s) -
Chi Celestine N.,
Gianni Stefano,
Calosci Nicoletta,
Travaglini-Allocatelli Carlo,
Engström Åke,
Jemth Per
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.011
Subject(s) - pdz domain , folding (dsp implementation) , protein folding , kinetics , chemistry , biophysics , topology (electrical circuits) , protein superfamily , crystallography , biology , physics , biochemistry , gene , mathematics , quantum mechanics , combinatorics , electrical engineering , engineering
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 p ostsynaptic density protein‐95, d isc‐large tumor suppressor protein, z onula 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 β T ‐values) are fairly constant for the five PDZ domains.