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Related Concept Videos

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.
1.8K
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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¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

2.2K
The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
2.2K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

1.6K
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.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
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Temperature-resistant bicelles for structural studies by solid-state NMR spectroscopy.

Kazutoshi Yamamoto1, Paige Pearcy, Dong-Kuk Lee

  • 1Department of Chemistry and Biophysics, University of Michigan , 930 N. University Ave., Ann Arbor, Michigan 48109-1055, United States.

Langmuir : the ACS Journal of Surfaces and Colloids
|January 8, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed temperature-resistant bicelles using specific lipids (DDPC and DHepPC) for membrane protein structure determination. These stable bicelles maintain protein folding and enhance solid-state NMR sensitivity across a wide temperature range.

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High-throughput Crystallization of Membrane Proteins Using the Lipidic Bicelle Method
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High-throughput Crystallization of Membrane Proteins Using the Lipidic Bicelle Method

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Determining membrane protein structures is crucial for understanding biological functions.
  • Challenges exist in maintaining native folding and function outside the cell membrane, especially for proteins with large soluble domains.
  • Conventional micelles have limitations for structural studies, and while bicelles offer improvements, their thermal instability is a significant drawback.

Purpose of the Study:

  • To overcome the temperature restrictions of bicelles for membrane protein structural studies.
  • To identify optimal bicellar compositions for enhanced stability and broad temperature applicability.
  • To demonstrate the utility of these temperature-resistant bicelles in solid-state NMR experiments.

Main Methods:

  • Investigated bicelle compositions using 1,2-didecanoyl-sn-glycero-3-phosphocholine (DDPC) and 1,2-diheptanoyl-sn-glycero-3-phosphocholin (DHepPC).
  • Assessed bicelle stability and magnetic alignment over a temperature range of -15 to 80 °C.
  • Utilized two-dimensional separated-local field (SLF) solid-state NMR experiments on cytochrome b5 incorporated in aligned bicelles.
  • Employed (31)P NMR experiments to characterize bicellar morphology, q ratio/size, and hydration levels.

Main Results:

  • Identified DDPC and DHepPC bicelles as stable and resistant to temperature variations without additional stabilizers.
  • Demonstrated robust bicellar phase and magnetic alignment across a broad temperature range (-15 to 80 °C).
  • Showcased the retention of native membrane protein structure and increased sensitivity in low-temperature solid-state NMR experiments.
  • Provided morphological information on DDPC-based bicelles, valuable for various biophysical and spectroscopic techniques.

Conclusions:

  • Developed novel, temperature-resistant bicelles composed of DDPC and DHepPC that overcome limitations of conventional systems.
  • These bicelles are suitable for structural studies of membrane proteins, including those with large soluble domains, across a wide temperature spectrum.
  • The findings enhance the applicability of solid-state NMR, particularly at low temperatures, for membrane protein structure determination and biophysical investigations.