Evidence map›Paper›PMID 26523621›Full record

ArticleBiochemistry2015

Helix-Capping Histidines: Diversity of N-H···N Hydrogen Bond Strength Revealed by (2h)JNN Scalar Couplings.

Matthew R Preimesberger, Ananya Majumdar, Selena L Rice, Lauren Que, Juliette T J Lecomte

Abstract read
In one paragraph

Article in Biochemistry, 2015. 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. Article
  2. Article
  3. The Iconic α-Helix: From Pauling to the Present.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Direct evidence for a deprotonated lysine serving as a H-bond "acceptor" in a photoreceptor protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Site-selectiveJournal of biomolecular NMR · 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

5 authors.

Matthew R PreimesbergerT. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.
Ananya MajumdarBiomolecular NMR Center, Johns Hopkins University , Baltimore, Maryland 21218, United States.
Selena L RiceT. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.
Lauren QueT. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.
Juliette T J LecomteT. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

In addition to its well-known roles as an electrophile and general acid, the side chain of histidine often serves as a hydrogen bond (H-bond) acceptor. These H-bonds provide a convenient pH-dependent switch for local structure and functional motifs. In hundreds of instances, a histidine caps the N-terminus of α- and 310-helices by forming a backbone NH···Nδ1 H-bond. To characterize the resilience and dynamics of the histidine cap, we measured the trans H-bond scalar coupling constant, (2h)JNN, in several forms of Group 1 truncated hemoglobins and cytochrome b5. The set of 19 measured (2h)JNN values were between 4.0 and 5.4 Hz, generally smaller than in nucleic acids (~6-10 Hz) and indicative of longer, weaker bonds in the studied proteins. A positive linear correlation between (2h)JNN and the difference in imidazole ring (15)N chemical shift (Δ(15)N = |δ(15)Nδ1 - δ(15)Nε2|) was found to be consistent with variable H-bond length and variable cap population related to the ionization of histidine in the capping and noncapping states. The relative ease of (2h)JNN detection suggests that this parameter can become part of the standard arsenal for describing histidines in helix caps and other key structural and catalytic elements involving NH···N H-bonds. The combined nucleic acid and protein data extend the utility of (2h)JNN as a sensitive marker of local structural, dynamic, and thermodynamic properties in biomolecules.

Indexed as

Bacterial ProteinsChlamydomonasCytochromes b5HemeHemoglobinsHistidineHydrogen BondingMethemoglobinModels, MolecularNuclear Magnetic Resonance, BiomolecularProteinsProtein Structure, SecondaryRecombinant ProteinsSynechococcusSynechocystisTruncated HemoglobinsBacterial ProteinscyanomethemoglobinCytochromes b5GlbN protein, bacteriaHemeHemoglobinsHistidineMethemoglobinProteinsRecombinant Proteinsslr2097 protein, SynechocystisTruncated Hemoglobins

Identifiers

PMID26523621
PMCPMC4660981

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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.