@article{50cb2eab8b63460290ca926c4f78f2df,
title = "The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein",
abstract = "Background: Residue 138 situates in the hinge region connecting the DNA- and cAMP-binding domains of CRP. Results: A correlation was established among N-capping propensities and cooperativity of cAMP binding and affinity for lac-DNA. Conclusion: Our results provide a quantitative characterization of the N-capping properties of residue 138 in the allosteric activation event. Significance: The results provide the thermodynamic basis to the structural model of allostery.",
author = "Shaoning Yu and Maillard, {Rodrigo A.} and Gribenko, {Alexey V.} and Lee, {J. Ching}",
note = "Funding Information: * This work was supported, in whole or in part, by National Institutes of Health Grant GM-77551. This work was also supported by the Robert A. Welch Foundation. 1 Present address: Fudan University, Shanghai 200433, China. 2 Present address: University of California at Berkeley, CA. 3 Present address: Pfizer, Inc., New York, NY. 4 To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, The University of Texas Medical Branch at Galveston, Galveston, TX 77555-1055. Tel.: 409-772-2281; Fax: 409-772-4298; E-mail: jclee@utmb.edu. 5The abbreviations used are: CRP, cAMP receptor protein; H/D, hydrogen/ deuterium; ITC, isothermal titration calorimetry. Publisher Copyright: {\textcopyright} 2012 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.",
year = "2012",
month = nov,
day = "16",
doi = "10.1074/jbc.M112.404806",
language = "English (US)",
volume = "287",
pages = "39402--39411",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "47",
}