Evidence map›Paper›PMID 28553525›Full record

ArticleChemical science2017

The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts.

Christopher R Walters, D Miklos Szantai-Kis, Yitao Zhang, Zachary E Reinert, W Seth Horne, David M Chenoweth, E James Petersson

Abstract read
In one paragraph

Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
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  11. Thioamide Analogues of MHC I Antigen Peptides.Journal of the American Chemical Society · 2023
    Article
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  13. Article
  14. Article
  15. Article
  16. Article
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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.

Christopher R WaltersDepartment of Chemistry , University of Pennsylvania , 231 S. 34th Street , Philadelphia , PA 19104 , USA.ORCID 0000-0003-2938-6034
D Miklos Szantai-KisBiochemistry and Molecular Biophysics Graduate Group , University of Pennsylvania , 3700 Hamilton Walk , Philadelphia , PA 19104 , USA.ORCID 0000-0001-5958-5478
Yitao ZhangDepartment of Chemistry , University of Pennsylvania , 231 S. 34th Street , Philadelphia , PA 19104 , USA.ORCID 0000-0002-1922-3955
Zachary E ReinertDepartment of Chemistry , University of Pittsburgh , 219 Parkman Avenue , Pittsburgh , PA 15260 , USA.ORCID 0000-0002-9192-043X
W Seth HorneDepartment of Chemistry , University of Pittsburgh , 219 Parkman Avenue , Pittsburgh , PA 15260 , USA.ORCID 0000-0003-2927-1739
David M ChenowethDepartment of Chemistry , University of Pennsylvania , 231 S. 34th Street , Philadelphia , PA 19104 , USA.ORCID 0000-0002-0819-4669
E James PeterssonDepartment of Chemistry , University of Pennsylvania , 231 S. 34th Street , Philadelphia , PA 19104 , USA.ORCID 0000-0003-3854-9210

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Molecular Mimics of Protein Tertiary Folding from Primary Sequence InformationR01GM107161 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HORNE, WILLIAM SETH · 2013 to 2022
$2.6M
Time-Of-Flight Instrument with Variable Ionization SourcesS10RR023444 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2007 to 2007
$308k
NCRR NIH HHS S10 RR023444NIGMS NIH HHS R01 GM107161NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Thioamides are single atom substitutions of the peptide bond that serve as versatile probes of protein structure. Effective use of thioamides requires a robust understanding of the impact that the substitution has on a protein of interest. However, the thermodynamic effects of thioamide incorporation have only been studied in small structural motifs, and their influence on secondary structure in the context of full-length proteins is not known. Here we describe a comprehensive survey of thioamide substitutions in three benchmark protein systems (calmodulin, the B1 domain of protein G, and collagen) featuring the most prevalent secondary structure motifs: α-helix, β-sheet, and polyproline type II helix. We find that in most cases, effects on thermostability can be understood in terms of the positioning and local environment of the thioamide relative to proximal structural elements and hydrogen bonding networks. These observations set the stage for the rational design of thioamide substituted proteins with predictable stabilities.

Identifiers

PMID28553525
PMCPMC5428018

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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.