Evidence map›Paper›PMID 33148530›Full record

ReviewBiochimica et biophysica acta. Proteins and proteomics2021

Low barrier hydrogen bonds in protein structure and function.

M Trent Kemp, Eric M Lewandowski, Yu Chen

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Proteins and proteomics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure of Bovine GlycineBiochemistry · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Unusually Rapid Isomerization of Aspartic Acid in Tau.bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

M Trent KempDepartment of Molecular Medicine, University of South Florida Morsani College of Medicine, 12901 Bruce B. Downs Blvd, MDC 3522, Tampa, Florida 33612, United States.
Eric M LewandowskiDepartment of Molecular Medicine, University of South Florida Morsani College of Medicine, 12901 Bruce B. Downs Blvd, MDC 3522, Tampa, Florida 33612, United States.
Yu ChenDepartment of Molecular Medicine, University of South Florida Morsani College of Medicine, 12901 Bruce B. Downs Blvd, MDC 3522, Tampa, Florida 33612, United States. Electronic address: ychen1@usf.edu.
University of South Florida · US

Funding

Novel inhibitor discovery against Pseudomonas aeruginosa PBP3R21AI147654 · NIAID · UNIVERSITY OF SOUTH FLORIDA · PI CHEN, YU · 2019 to 2020
$411k
NIAID NIH HHS R21 AI147654
6 · The paper itself

Abstract

Low-barrier hydrogen bonds (LBHBs) are a special type of short hydrogen bond (HB) that is characterized by the equal sharing of a hydrogen atom. The existence and catalytic role of LBHBs in proteins has been intensely contested. Advancements in X-ray and neutron diffraction methods has revealed delocalized hydrogen atoms involved in potential LBHBs in a number of proteins, while also demonstrating that short HBs are not necessarily LBHBs. More importantly, a series of experiments on ketosteroid isomerase (KSI) have suggested that LBHBs are significantly stronger than standard HBs in the protein microenvironment in terms of enthalpy, but not free energy. The discrepancy between the enthalpy and free energy of LBHBs offers clues to the challenges, and potential solutions, of the LBHB debate, where the unique strength of LBHBs plays a special role in the kinetic processes of enzyme function and structure, together with other molecular forces in a pre-organized environment.

Indexed as

BiocatalysisAnimalsBacteriaHumansHydrogenHydrogen BondingPlantsProtein ConformationProteinsSaccharomyces cerevisiaeSteroid IsomerasesStructure-Activity RelationshipThermodynamicsHydrogenProteinsSteroid IsomerasesEnzyme catalysisLBHBNeutron diffractionNMR downfield shiftShort HBSub-angstrom resolution X-ray crystallography

Identifiers

PMID33148530
PMCPMC7736181
OpenAlexW3093723493

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.