ArticleARKIVOC : free online journal of organic chemistry2010
Modulation of an n→π* interaction with α-fluoro groups.
Article in ARKIVOC : free online journal of organic chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
The trial behind it
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Who cites it
10 citing papers in PubMed.
- Electronic and Steric Control of n→π* Interactions: Stabilization of the α-Helix Conformation without a Hydrogen Bond.Chembiochem : a European journal of chemical biology · 2019Article
- The n→π* Interaction.Accounts of chemical research · 2017Article
- Reciprocal carbonyl-carbonyl interactions in small molecules and proteins.Nature communications · 2017Article
- n→π* interactions engender chirality in carbonyl groups.Organic letters · 2014Article
- A key n→π* Interaction in N-acyl homoserine lactones.ACS chemical biology · 2014Article
- Synthesis and biological evaluation of novel N-α-haloacylated homoserine lactones as quorum sensing modulators.Beilstein journal of organic chemistry · 2014Article
- Pyramidalization of a carbonyl C atom in (2S)-N-(seleno-acet-yl)proline methyl ester.Acta crystallographica. Section E, Structure reports online · 2013Article
- Intimate interactions with carbonyl groups: dipole-dipole or n→π*?The Journal of organic chemistry · 2013Article
- A conserved interaction with the chromophore of fluorescent proteins.Protein science : a publication of the Protein Society · 2012Article
- An evaluation of peptide-bond isosteres.Chembiochem : a European journal of chemical biology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Noncovalent interactions play an essential role in biological and chemical processes. In the main chain of common protein secondary structures, the lone pair (n) of a carbonyl oxygen is delocalized into the antibonding orbital (π*) of the subsequent carbonyl group. Herein, experimental and computational data reveal that this n→π* interaction can be attenuated by the inductive electron withdrawal of one or two α-fluoro groups in the donor. The steric effect of three α-fluoro groups, however, overcomes the inductive withdrawal. These data evoke a means to modulate the n→π* interaction in peptides, proteins, and other systems.
Identifiers
21643549PMC3107012What OpenQuestion holds
Registered trials
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.