Evidence map›Paper›PMID 22844177›Full record

ArticleChemical physics2011

A peptide's perspective of water dynamics.

Ayanjeet Ghosh, Robin M Hochstrasser

Abstract read
In one paragraph

Article in Chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  11. Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO).Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Ester carbonyl vibration as a sensitive probe of protein local electric field.Angewandte Chemie (International ed. in English) · 2014
    Article
  13. Article
  14. 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.

Ayanjeet GhoshDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Robin M Hochstrasser
University of Pennsylvania · US

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Ultrafast Processing in Proteins and Other AssembliesR01GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 1985 to 2013
$3.5M
ULTRAFAST PROCESSES IN PROTEINS AND OTHER ASSEMBLIESR37GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1992 to 2001
$493k
NCRR NIH HHS P41 RR001348NIGMS NIH HHS R01 GM012592NIGMS NIH HHS R37 GM012592
6 · The paper itself

Abstract

This Perspective is focused on amide groups of peptides interacting with water. The 2D IR spectroscopy has already enabled structural aspects of the peptide backbone to be determined through its ability to measure the coupling between different amide-I modes. Here we describe why nonlinear IR is emerging as the method of choice to examine the fast components of the water dynamics near peptides and how isotopically edited peptide links can be used to probe the local water at a residue level in proteins. This type of research necessarily involves an intimate mix of theory and experiment. The description of the results is underpinned by relatively well established quantum-statistical theories that describe the important manifestations of peptide vibrational frequency fluctuations.

Identifiers

PMID22844177
PMCPMC3404498
OpenAlexW2066398728

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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.