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Related Concept Videos

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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NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
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Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
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Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

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The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

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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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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.4K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Characterization of membrane protein function by solid-state NMR spectroscopy.

Lindsay A Baker1, Marc Baldus1

  • 1NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands.

Current Opinion in Structural Biology
|May 29, 2014
PubMed
Summary
This summary is machine-generated.

Solid-state nuclear magnetic resonance spectroscopy (ssNMR) helps determine membrane protein structure and function. This review highlights ssNMR applications for diverse membrane proteins, aiding biological insights.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Membrane proteins are crucial for cellular functions but challenging to study structurally due to their lipid bilayer association and mobility.
  • Diverse experimental techniques require different membrane mimetics, complicating the correlation of structure to function.
  • High-resolution structural studies of membrane proteins are essential for understanding their biological roles.

Purpose of the Study:

  • To review the application of solid-state nuclear magnetic resonance spectroscopy (ssNMR) for correlating membrane protein structure and function.
  • To discuss diverse biological roles of membrane proteins, including signaling, transport, and enzymatic reactions, studied using ssNMR.
  • To explore complementary information sources and implications for biology derived from ssNMR studies.

Main Methods:

  • Solid-state nuclear magnetic resonance spectroscopy (ssNMR) is the primary technique discussed.
  • Examples of ssNMR experiments used for membrane protein structure determination are presented.
  • Complementary experimental techniques and data analysis strategies are considered.

Main Results:

  • ssNMR enables the correlation of structure and function in membrane proteins with various biological roles.
  • The review provides examples of ssNMR applications across different membrane protein classes.
  • Understanding membrane protein dynamics and interactions is facilitated by ssNMR.

Conclusions:

  • ssNMR is a powerful tool for elucidating membrane protein structure-function relationships.
  • The review discusses the implications of ssNMR findings for broader biological understanding.
  • Future directions include extending ssNMR studies to native cellular environments.