Evidence map›Paper›PMID 26621709›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Protein-like proton exchange in a synthetic host cavity.

William M Hart-Cooper, Carmelo Sgarlata, Charles L Perrin, F Dean Toste, Robert G Bergman, Kenneth N Raymond

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. An isolated water droplet in the aqueous solution of a supramolecular tetrahedral cage.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Excitation Energy Delocalization and Transfer to Guests within MJournal of the American Chemical Society · 2017
    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

6 authors.

William M Hart-CooperChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720;
Carmelo SgarlataChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720;
Charles L PerrinDepartment of Chemistry & Biochemistry, University of California, San Diego, La Jolla, CA 92093.
F Dean TosteChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720; fdtoste@berkeley.edu rbergman@berkeley.edu raymond@socrates.berkeley.edu.
Robert G BergmanChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720; fdtoste@berkeley.edu rbergman@berkeley.edu raymond@socrates.berkeley.edu.
Kenneth N RaymondChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720; fdtoste@berkeley.edu rbergman@berkeley.edu raymond@socrates.berkeley.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of proton exchange in a metal-ligand enzyme active site mimic (compound 1) is described through amide hydrogen-deuterium exchange kinetics. The type and ratio of cationic guest to host in solution affect the rate of isotope exchange, suggesting that the rate of exchange is driven by a host whose cavity is occupied by water. Rate constants for acid-, base-, and water-mediated proton exchange vary by orders of magnitude depending on the guest, and differ by up to 200 million-fold relative to an alanine polypeptide. These results suggest that the unusual microenvironment of the cavity of 1 can dramatically alter the reactivity of associated water by magnitudes comparable to that of enzymes.

Indexed as

Deuterium Exchange MeasurementProtonsAlanineAmidesEnzymesHydrogen BondingHydrogen-Ion ConcentrationKineticsModels, MolecularProteinsSolutionsTime FactorsWaterAlanineAmidesEnzymesProteinsProtonsSolutionsWatercatalysishydrogen–deuterium exchangenoncovalentprotonsupramolecular

Identifiers

PMID26621709
PMCPMC4687555

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.