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• W1999857568 abstract "Inhibitory helix 1 (HI-1) of the Ets-1 human transcription factor unfolds upon binding the target DNA sequence. To identify the interactions that stabilize HI-1 in the apo state, we performed replica exchange and molecular dynamics simulations of various apo Ets-1 constructs. The simulations indicate the importance of local interactions for the stability of HI-1. The HI-2 and H4 helices stabilize the helical state of HI-1 through specific residue-residue contacts and macrodipolar interactions. The amount of stabilization in small length HI-1+H2 and HI-1+H4 constructs was similar to that in the protein. The studies suggest that the partial unfolding of Ets-1 upon DNA binding can be achieved by the removal of just a few specific local contacts." @default.
• W1999857568 created "2016-06-24" @default.
• W1999857568 creator A5012698288 @default.
• W1999857568 creator A5027580418 @default.
• W1999857568 date "2012-05-01" @default.
• W1999857568 modified "2023-10-17" @default.
• W1999857568 title "Importance of local interactions for the stability of inhibitory helix 1 in apo Ets-1" @default.
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• W1999857568 doi "https://doi.org/10.1016/j.bpc.2012.03.007" @default.
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