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Related Concept Videos

Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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...
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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.
The...
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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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Rapid Scan Electron Paramagnetic Resonance Opens New Avenues for Imaging Physiologically Important Parameters In Vivo
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Published on: September 26, 2016

FAST-NMR: functional annotation screening technology using NMR spectroscopy.

Kelly A Mercier1, Michael Baran, Viswanathan Ramanathan

  • 1Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, USA.

Journal of the American Chemical Society
|November 23, 2006
PubMed
Summary
This summary is machine-generated.

A novel FAST-NMR method uses protein-ligand interactions to determine the function of unknown proteins. This approach analyzes active sites to identify biological roles, even without sequence similarity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Biology

Background:

  • Structural genomics and the Protein Structure Initiative (PSI) generate many protein structures lacking clear functional annotations due to absent sequence or structural homology.
  • Assigning functions to these novel proteins is crucial for understanding biological pathways and developing new therapeutics.

Purpose of the Study:

  • To develop and demonstrate a high-throughput Nuclear Magnetic Resonance (NMR) methodology, termed FAST-NMR, for annotating the biological function of uncharacterized proteins.
  • To leverage protein-ligand interactions as a basis for functional assignment, independent of global sequence or structural similarity.

Main Methods:

  • A tiered NMR screening approach using a library of biologically active compounds to identify protein-ligand interactions.
  • Determining a rapid co-structure by integrating NMR chemical shift perturbation data (identifying ligand binding sites) with AutoDock protein-ligand docking.
  • Utilizing CPASS (Comparison of Protein Active Site Structures) software and database to compare identified active sites against a database of proteins with known functions.

Main Results:

  • The FAST-NMR methodology successfully identified potential functional roles for unannotated proteins by analyzing their ligand-binding active sites.
  • The approach demonstrated its efficacy using the unannotated protein SAV1430 from Staphylococcus aureus as a test case.
  • The integration of experimental NMR data with computational docking and database comparison provided a robust method for functional annotation.

Conclusions:

  • FAST-NMR offers a powerful high-throughput solution for assigning functions to novel proteins emerging from structural genomics efforts.
  • The principle that similar functions correlate with similar active site and ligand-binding interactions holds true, even for proteins with divergent global structures.
  • This methodology significantly advances the ability to annotate the proteome and understand protein function in the absence of traditional homology information.