Evidence map›Paper›PMID 28375734›Full record

ReviewAnnual review of biophysics2017

High-Dimensional Mutant and Modular Thermodynamic Cycles, Molecular Switching, and Free Energy Transduction.

Charles W Carter

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Microcalorimetry reveals multi-state thermal denaturation ofStructural dynamics (Melville, N.Y.) · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Coding of Class I and II Aminoacyl-tRNA Synthetases.Advances in experimental medicine and biology · 2017
    Review
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

1 author at 1 institution in 1 country.

Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27514; email: carter@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Sense/Antisense Genetic Coding and the Origins of TranslationR01GM078227 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2006 to 2018
$3.9M
Storage and Recovery of ATP binding energy in Metal-Catalyzed Phosphoryl-TransferR01GM090406 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2010 to 2013
$1.4M
NIGMS NIH HHS R01 GM078227NIGMS NIH HHS R01 GM090406
6 · The paper itself

Abstract

Understanding how distinct parts of proteins produce coordinated behavior has driven and continues to drive advances in protein science and enzymology. However, despite consensus about the conceptual basis for allostery, the idiosyncratic nature of allosteric mechanisms resists general approaches. Computational methods can identify conformational transition states from structural changes, revealing common switching mechanisms that impose multistate behavior. Thermodynamic cycles use factorial perturbations to measure coupling energies between side chains in molecular switches that mediate shear during domain motion. Such cycles have now been complemented by modular cycles that measure energetic coupling between separable domains. For one model system, energetic coupling between domains has been shown to be quantitatively equivalent to that between dynamic side chains. Linkages between domain motion, switching residues, and catalysis make nucleoside triphosphate hydrolysis conditional on domain movement, confirming an essential yet neglected aspect of free energy transduction and suggesting the potential generality of these studies.

Indexed as

Allosteric RegulationBiocatalysisHydrolysisIon Channel GatingModels, BiologicalModels, MolecularMolecular ConformationMutationNucleotidesPotassium Channels, Voltage-GatedProtein DomainsThermodynamicsTryptophan-tRNA LigaseNucleotidesPotassium Channels, Voltage-GatedTryptophan-tRNA Ligasecatalysisdomain motiontryptophanyl-tRNA synthetasevoltage-gated K+ channel

Identifiers

PMID28375734
PMCPMC5472044
OpenAlexW2604855319

What OpenQuestion 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 OpenQuestion graph.