Evidence map›Paper›PMID 37624071›Full record

ArticleProtein science : a publication of the Protein Society2023

Site-specific relaxation of peptide bond planarity induced by electrically attracted proton/deuteron observed by neutron crystallography.

Kaori Chiba, Takuro Matsui, Toshiyuki Chatake, Takashi Ohhara, Ichiro Tanaka, Katsuhide Yutani, Nobuo Niimura

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Neutron crystallography of the covalent intermediate of β-glucosidase reveals remodeling of the catalytic center.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. 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

7 authors.

Kaori ChibaAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.ORCID 0000-0002-0081-558X
Takuro MatsuiAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.
Toshiyuki ChatakeAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.
Takashi OhharaAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.
Ichiro TanakaAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.
Katsuhide YutaniRIKEN SPring-8 Center, Sayo, Hyogo, Japan.
Nobuo NiimuraAdvanced Science Research Centre, JAERI, Tokai, Ibaraki, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In structural biology, peptide bonds, fundamental linkages between hundreds of amino acids, of which a protein molecule is composed, have been commonly treated as a plane structure just as Linus Pauling et al. proposed. In this paper, a site-specific peptide bond relaxation mechanism by deuterons whose localization has been suggested by neutron crystallography is proposed. Such deuteron was observed as an arm of neutron scattering length density protruding from the carbonyl oxygen atoms in the main chain in the omit map drawn by neutron crystallography of human lysozyme. Our comprehensive study using x-ray and neutron diffraction and

Indexed as

Neutron DiffractionProtonsCrystallographyCrystallography, X-RayDeuteriumHumansHydrogen BondingNeutronsPeptidesDeuteriumPeptidesProtonsacidic amino acidelectrostatic potentialmain chainneutron diffractionNMRpeptide bond planarityx-ray diffraction

Identifiers

PMID37624071
PMCPMC10510461

What OpenQuestion holds

Textmetadata
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.