ArticleBiochemistry2015
Helix-Capping Histidines: Diversity of N-H···N Hydrogen Bond Strength Revealed by (2h)JNN Scalar Couplings.
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.
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Who cites it
11 citing papers in PubMed.
- A structural bioinformatics framework for prioritizing pH-sensitive proteins from 3D structural features.BMC bioinformatics · 2026Article
- [Tripeptide polymer-based cell-imprinted hydrogels for high-efficiency circulating tumor cell capture].Se pu = Chinese journal of chromatography · 2026Article
- The Iconic α-Helix: From Pauling to the Present.Methods in molecular biology (Clifton, N.J.) · 2025Article
- 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 · 2024Article
- Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation.Journal of the American Chemical Society · 2024Article
- Detecting the Hydrogen Bond Cooperativity in a Protein β-Sheet by H/D Exchange.International journal of molecular sciences · 2022Article
- Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii.Biochimica et biophysica acta. General subjects · 2018Article
- Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.Biochemistry · 2018Article
- Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.Biochemistry · 2018Article
- Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
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5 authors.
Funding
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.
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