Price of disorder in the lac repressor hinge helix

Danielle Seckfort, Bernard Pettitt

Research output: Contribution to journalArticle

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 1 2019

Fingerprint

Lac Repressors
Hinges
Repressor Proteins
Proteins
Lac Operon
DNA sequences
Gene expression
Conformations
Salts
Genes
DNA

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Price of disorder in the lac repressor hinge helix. / Seckfort, Danielle; Pettitt, Bernard.

In: Biopolymers, Vol. 110, No. 1, e23239, 01.01.2019.

Research output: Contribution to journalArticle

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