Evidence map›Paper›PMID 27059978›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

"Wet" Versus "Dry" Folding of Polyproline.

Liuqing Shi, Alison E Holliday, Brian C Bohrer, Doyong Kim, Kelly A Servage, David H Russell, David E Clemmer

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Review
  3. Memory Effect in Thermoresponsive Proline-based Polymers.Angewandte Chemie (International ed. in English) · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016
    Article
  10. Structures of the kinetically trapped i-motif DNA intermediates.Physical chemistry chemical physics : PCCP · 2016
    Article
  11. Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016
    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.

Liuqing ShiDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Alison E HollidayDepartment of Chemistry, Moravian College, Bethlehem, PA, 18018, USA.
Brian C BohrerDepartment of Chemistry, University of Southern Indiana, Evansville, IN, 47712, USA.
Doyong KimDepartment of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
Kelly A ServageDepartment of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
David H RussellDepartment of Chemistry, Texas A&M University, College Station, TX, 77843, USA. russell@chem.tamu.edu.
David E ClemmerDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA. Clemmer@Indiana.EDU.

Funding

Computational approaches to protein identification and quantification using MS/MSR01GM103725 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI RADIVOJAC, PREDRAG · 2012 to 2015
$1.7M
NIGMS NIH HHS R01 GM103725
6 · The paper itself

Abstract

When the all-cis polyproline-I helix (PPI, favored in 1-propanol) of polyproline-13 is introduced into water, it folds into the all-trans polyproline-II (PPII) helix through at least six intermediates [Shi, L., Holliday, A.E., Shi, H., Zhu, F., Ewing, M.A., Russell, D.H., Clemmer, D.E.: Characterizing intermediates along the transition from PPI to PPII using ion mobility-mass spectrometry. J. Am. Chem. Soc. 136, 12702-12711 (2014)]. Here, we show that the solvent-free intermediates refold into the all-cis PPI helix with high (>90%) efficiency. Moreover, in the absence of solvent, each intermediate appears to utilize the same small set of pathways observed for the solution-phase PPII → PPI transition upon immersion of PPIIaq in 1-propanol. That folding in solution (under conditions where water is displaced by propanol) and folding in vacuo (where energy required for folding is provided by collisional activation) occur along the same pathway is remarkable. Implicit in this statement is that 1-propanol mimics a "dry" environment, similar to the gas phase. We note that intermediates with structures that are similar to PPIIaq can form PPII under the most gentle activation conditions-indicating that some transitions observed in water (i.e., "wet" folding, are accessible (albeit inefficient) in vacuo. Lastly, these "dry" folding experiments show that PPI (all cis) is favored under "dry" conditions, which underscores the role of water as the major factor promoting preference for trans proline. Graphical Abstract ᅟ.

Indexed as

Protein FoldingPeptidesProlineProtein Structure, SecondarySolventsThermodynamicsPeptidespolyprolineProlineSolventsCollisional activationFolding

Identifiers

PMID27059978
PMCPMC5152579

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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.