@article{ea48952aeafb403baf684fbdd8878d60,
title = "Price of disorder in the lac repressor hinge helix",
abstract = "The Lac system of genes has been pivotal in understanding gene regulation. When the lac repressor protein binds to the correct DNA sequence, the hinge region of the protein goes through a disorder to order transition. The structure of this region of the protein is well understood when it is in this bound conformation, but less so when it is not. Structural studies show that this region is flexible. Our simulations show this region is extremely flexible in solution; however, a high concentration of salt can help kinetically trap the hinge helix. Thermodynamically, disorder is more favorable without the DNA present.",
keywords = "LacI, MD simulations, disorder to order transition, disordered proteins, metadynamics, protein, salt stability",
author = "Danielle Seckfort and {Montgomery Pettitt}, B.",
note = "Funding Information: National Institute of General Medical Sciences, Grant/Award Number: GM-037657; National Science Foundation, Grant/Award Numbers: CNS-1338192, ACI-1548562; National Institutes of Health; Robert A. Welch Foundation, Grant/Award Number: GM-037657 Funding Information: information: National Institute of General Medical Sciences, Grant/Award Number: GM-037657; National Science Foundation, Grant/Award Numbers: CNS-1338192, ACI-1548562; National Institutes of Health; Robert A. Welch Foundation, Grant/Award Number: GM-037657The authors thank Dr.s Cheng Zhang and Gillian Lynch for many helpful discussions. The Sealy Center for Structural Biology scientific computing staff is acknowledged for computational support. We gratefully acknowledge the Robert A. Welch Foundation (H-0037), and the National Institutes of Health (GM-037657) for partial support of this work. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. The authors also acknowledge the Texas Advanced Computing Center (TACC) at The University of Texas at Austin for providing HPC resources that have contributed to the research results reported within this article. URL: http://www.tacc.utexas.edu Visualization was aided by a grant from NSF (CNS-1338192). Funding Information: The authors thank Dr.s Cheng Zhang and Gillian Lynch for many helpful discussions. The Sealy Center for Structural Biology scientific computing staff is acknowledged for computational support. We gratefully acknowledge the Robert A. Welch Foundation (H-0037), and the National Institutes of Health (GM-037657) for partial support of this work. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. The authors also acknowledge the Texas Advanced Computing Center (TACC) at The University of Texas at Austin for providing HPC resources that have contributed to the research results reported within this article. URL: http://www. tacc.utexas.edu Visualization was aided by a grant from NSF (CNS-1338192). Publisher Copyright: {\textcopyright} 2018 Wiley Periodicals, Inc.",
year = "2019",
month = jan,
doi = "10.1002/bip.23239",
language = "English (US)",
volume = "110",
journal = "Biopolymers",
issn = "0006-3525",
publisher = "John Wiley and Sons Inc.",
number = "1",
}