The trigger sequence in the GCN4 leucine zipper:
-helical propensity and multistate dynamics of folding and dimerization
J. Chem. Phys. 129, 175103 (2008); doi:10.1063/1.3006421
Published 7 November 2008
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We investigate the importance of the trigger sequence in the folding and dimerization of the GCN4 leucine zipper. We examine the role of the enhanced propensity of the amino acids in the trigger sequence to form an
-helix. Using computer simulations, we calculate heat capacities, free energy profiles, and the probability for successful dimerization as a function of the strength of the
-helical propensity of the trigger sequence. Our results elucidate the experimentally observed importance of the trigger sequence for dimerization and why it is not necessary for the trigger to have a specific “consensus” sequence of amino acids. We also find that a stronger trigger sequence not only increases the probability for dimerization but also changes the dimerization dynamics by introducing multiple intermediate states.
©2008 American Institute of Physics
-helix. Using computer simulations, we calculate heat capacities, free energy profiles, and the probability for successful dimerization as a function of the strength of the
-helical propensity of the trigger sequence. Our results elucidate the experimentally observed importance of the trigger sequence for dimerization and why it is not necessary for the trigger to have a specific “consensus” sequence of amino acids. We also find that a stronger trigger sequence not only increases the probability for dimerization but also changes the dimerization dynamics by introducing multiple intermediate states.
©2008 American Institute of Physics
| History: | Received 19 August 2008; accepted 3 October 2008; published 7 November 2008 |
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http://link.aip.org/link/?JCPSA6/129/175103/1 |
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