Evidence map›Paper›PMID 30485404›Full record

ArticleBiopolymers2019

Price of disorder in the lac repressor hinge helix.

Danielle Seckfort, B Montgomery Pettitt

Abstract read
In one paragraph

Article in Biopolymers, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 50% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Danielle SeckfortStructural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas.ORCID https://orcid.org/0000-0001-7235-7357
B Montgomery PettittStructural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas.ORCID https://orcid.org/0000-0003-4902-3046
Baylor College of Medicine · US

Funding

Theory of Proteins and Peptides in SolutionR01GM037657 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI PETTITT, BERNARD MONTGOMERY · 1988 to 2023
$5.5M
National Institute of General Medical Sciences GM-037657National Institutes of HealthNational Science Foundation ACI-1548562National Science Foundation CNS-1338192NIGMS NIH HHS R01 GM037657Robert A. Welch Foundation GM-037657
6 · The paper itself

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.

Indexed as

Protein ConformationBase SequenceDNA-Binding ProteinsEscherichia coliLac OperonLac RepressorsMolecular Dynamics SimulationNucleic Acid ConformationProtein DomainsProtein Structure, SecondaryDNA-Binding ProteinsLac Repressorsdisordered proteinsdisorder to order transitionLacIMD simulationsmetadynamicsproteinsalt stability

Identifiers

PMID30485404
PMCPMC6335174
OpenAlexW2903320452

What Socratic holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.