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Related Concept Videos

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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.0K
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...
1.0K
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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Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.1K
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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2D NMR: Overview of Homonuclear Correlation Techniques01:16

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Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
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Newman Projections02:06

Newman Projections

19.3K
Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as...
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Mapping conformational epitopes by NMR spectroscopy.

Ana P Valente1, Mariana Manzano-Rendeiro1

  • 1National NMR Center, Cenabio, Department of Structural Biology, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.

Current Opinion in Virology
|May 14, 2021
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic resonance (NMR) aids in mapping antibody binding sites, simplifying the development of targeted therapeutics like vaccines for viral infections and cancer.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Structural Biology

Background:

  • Antibodies are critical for pathogen neutralization and disease defense.
  • Antibodies are valuable tools for developing therapeutics against viral infections and cancer.
  • Current methods for developing specific antibodies are costly and time-consuming.

Purpose of the Study:

  • To discuss Nuclear Magnetic Resonance (NMR) approaches for conformational epitope mapping.
  • To highlight how structural and allosteric information can simplify antibody development.

Main Methods:

  • Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Analyzing protein structure and dynamics.
  • Applying NMR to study large protein complexes for epitope mapping.

Main Results:

  • NMR is an efficient technique for analyzing protein structure and dynamics.
  • NMR can overcome size limitations in studying large protein complexes.
  • NMR facilitates conformational epitope mapping.

Conclusions:

  • NMR-based methods offer an efficient way to map conformational epitopes.
  • Simplifying antibody development through structural insights.
  • Advancing therapeutic antibody design for various diseases.