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¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

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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...
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Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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Chemical Shift: Internal References and Solvent Effects01:17

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In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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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Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.8K
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.
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Metabolic transient studies by NMR.

T Binzoni1, G Ferretti, K Schenker

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International Journal of Sports Medicine
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Phosphocreatine hydrolysis in human muscles was measured using 31P-NMR spectroscopy. This study determined the half-time of oxygen consumption kinetics (t1/2 VO2) to be approximately 16 seconds.

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Area of Science:

  • Physiology
  • Biophysics
  • NMR Spectroscopy

Background:

  • Phosphocreatine (PC) hydrolysis is a key indicator of muscle energy metabolism.
  • 31P-NMR spectroscopy (31P-NMRS) allows non-invasive measurement of intracellular metabolites.
  • Understanding oxygen consumption (VO2) kinetics is crucial for assessing muscle aerobic capacity.

Purpose of the Study:

  • To measure the time course of phosphocreatine hydrolysis in human gastrocnemius muscle.
  • To derive the relationship between muscle oxygen consumption (VO2) and phosphocreatine ([PC]) using a bioenergetic model.
  • To directly estimate the half-time of intracellular VO2 kinetics (t1/2 VO2) in contracting human muscle.

Main Methods:

  • Utilized 31P-NMR spectroscopy (31P-NMRS) with a time resolution of 10.8 seconds.
  • Employed a bioenergetic model to relate muscle O2 consumption (VO2) to phosphocreatine ([PC]) levels.
  • Developed a procedure for correcting 31P-NMR spectra based on muscle temperature profiles obtained via proton imaging for low-temperature measurements.

Main Results:

  • The half-time of intracellular VO2 kinetics (t1/2 VO2) in the human gastrocnemius was found to be approximately 16 seconds.
  • This t1/2 VO2 was independent of the workload applied.
  • The determined t1/2 VO2 is comparable to the shortest values measured at the mouth, without lactate accumulation.

Conclusions:

  • The study successfully estimated the intracellular VO2 kinetics (t1/2 VO2) in human skeletal muscle.
  • The findings indicate a rapid aerobic response, with t1/2 VO2 around 16 seconds.
  • The developed methodology allows for the assessment of t1/2 VO2 even at low muscle temperatures.