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Related Concept Videos

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

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When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
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In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
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¹H NMR: Complex Splitting01:13

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
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Normalized and Directional Interplay Scoring for the Interrogation of Proteoform Data.

Karl F Poncha1, Alyssa T Paparella1, Nicolas L Young1,2

  • 1Verna & Marrs McLean Department of Biochemistry & Molecular Pharmacology, Baylor College of Medicine, Houston Texas.

Biorxiv : the Preprint Server for Biology
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Summary

New computational methods reveal histone proteoform dynamics during aging. Novel scores quantify post-translational modification (PTM) crosstalk, offering deeper insights into chromatin regulation and gene expression influenced by histone modifications.

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Area of Science:

  • Molecular Biology
  • Proteomics
  • Bioinformatics

Background:

  • Histone proteoforms, with multiple co-occurring post-translational modifications (PTMs), are crucial for chromatin regulation and gene expression.
  • Understanding histone proteoform dynamics is key to elucidating chromatin-based regulatory mechanisms.
  • Proteomics advances allow proteoform identification, but data complexity poses analytical challenges.

Purpose of the Study:

  • To introduce novel computational methods for analyzing histone PTM dynamics.
  • To develop and benchmark new scores for quantifying PTM crosstalk.
  • To apply these methods to study histone modifications in mouse organs during aging.

Main Methods:

  • Development of two novel PTM crosstalk scores: 'Normalized Interplay' and 'delta I' (Directional Interplay).
  • Benchmarking of the new scores against existing methods.
  • Application of a two-stage scoring approach to proteoform-level data from CrosstalkDB.

Main Results:

  • The 'Normalized Interplay' score provides a more complete and accurate measure of PTM crosstalk.
  • The 'delta I' score quantifies the magnitude and directionality of PTM crosstalk.
  • Analysis revealed dynamics of histone H3 modifications in mouse organs during aging.

Conclusions:

  • The developed computational methods and scores enhance the analysis of histone PTM dynamics.
  • These tools offer a more comprehensive understanding of PTM crosstalk and its role in biological processes like aging.
  • The findings contribute to the field of chromatin regulation and proteoform analysis.