Price of disorder in the lac repressor hinge helix

Danielle Seckfort, B. Montgomery Pettitt

Research output: Contribution to journalArticle

1 Scopus citations

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.

Original languageEnglish (US)
Article numbere23239
JournalBiopolymers
Volume110
Issue number1
DOIs
StatePublished - Jan 2019

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Keywords

  • LacI
  • MD simulations
  • disorder to order transition
  • disordered proteins
  • metadynamics
  • protein
  • salt stability

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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