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Related Concept Videos

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

804
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

1.1K
Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
1.1K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.0K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.0K

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Nanosecond Molecular Motion in pHP1α Liquid-Liquid Phase Separation Captured by Solid-State NMR.

Sze Yuet Chin1, Lei Zhao2, Yinglu Chen2,3

  • 1Centre of High Field NMR Spectroscopy and Imaging, Nanyang Technological University, 21 Nanyang Link, Singapore 637371.

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Phosphorylated heterochromatin protein 1 alpha (pHP1α) exhibits complex dynamics during liquid-liquid phase separation (LLPS). This study reveals ~15 ns motions, indicating distinct dynamic phases crucial for chromatin organization and genomic stability.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Dynamics

Background:

  • Protein structure, function, and dynamics are key to biological activity, especially in complex systems.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is vital for studying molecular motion across timescales.
  • Phase-separated systems, like phosphorylated heterochromatin protein 1 alpha (pHP1α), present unique challenges due to their mixed solid- and solution-like properties.

Purpose of the Study:

  • To investigate the nanosecond molecular motions within pHP1α liquid-liquid phase separation (LLPS).
  • To characterize the site-specific global dynamics of pHP1α during LLPS.
  • To understand the relationship between protein dynamics and chromatin organization.

Main Methods:

  • Utilized relaxation in hetNOE-filtered heteronuclear single quantum coherence (HSQC) signals to probe nanosecond dynamics.
  • Systematically analyzed motions using both hetNOE-filtered HSQC and conventional HSQC techniques.
  • Focused on site-specific analysis of molecular motion in pHP1α LLPS.

Main Results:

  • Identified approximately 15 nanosecond (ns) timescale motions in the pHP1α LLPS system.
  • Revealed evidence for the coexistence of different dynamic phases within pHP1α LLPS.
  • Findings align with and support previous observations regarding pHP1α's role in chromatin organization.

Conclusions:

  • The study elucidates the complex nanosecond dynamics of pHP1α during LLPS.
  • The detected motions suggest a heterogeneous dynamic environment within the phase-separated state.
  • This research enhances understanding of biomolecular phase separation, chromatin compaction, and genomic stability.