Integrative NMR for biomolecular research.
Woonghee Lee1, Gabriel Cornilescu2, Hesam Dashti2
1National Magnetic Resonance Facility at Madison and Biochemistry Department, University of Wisconsin-Madison, Madison, WI, 53706, USA. whlee@nmrfam.wisc.edu.
Journal of Biomolecular NMR
|March 30, 2016
Summary
This study introduces an accessible NMR platform, simplifying biomolecular NMR spectroscopy for non-specialists. The NMRFAM software and virtual machine integrate tools and tutorials for easier use.
Area of Science:
- Biochemistry
- Structural Biology
- Biophysics
Background:
- Nuclear Magnetic Resonance (NMR) spectroscopy is vital for elucidating biomolecular structure, function, and interactions in solution.
- The complexity of traditional NMR methods presents a barrier for researchers without specialized expertise.
Purpose of the Study:
- To develop and introduce an accessible platform that democratizes biomolecular NMR spectroscopy.
- To lower the barrier to entry for non-specialists using NMR for biological research.
Main Methods:
- Development of the NMRFAM software package, integrating essential tools, databases, and web services.
- Creation of a cross-platform virtual machine for easy deployment on standard computers.
- Provision of comprehensive video tutorials for guided learning and practical application.
Main Results:
- The NMRFAM platform significantly enhances the accessibility of biomolecular NMR spectroscopy.
- The integrated software and virtual machine streamline the process of data acquisition and analysis.
- Free availability of the software and tutorials promotes wider adoption.
Conclusions:
- The NMRFAM platform effectively addresses the complexity challenges in biomolecular NMR spectroscopy.
- This initiative empowers a broader range of scientists to utilize NMR for studying biomolecules.
- The platform facilitates real-time observation of molecular interactions and structural features.
Keywords:
Automated spectral analysisAutomated structure determination and validationChemical shift assignment and validationPeak identificationRestraint visualization and validationVisualization of spectra, assignments, and structuresMore Related Videos
Related Concept Videos
¹H NMR Signal Integration: Overview
4.0K
The intensity of a signal, which can be represented by the area under the peak, depends on the number of protons contributing to that signal. The area under each peak is shown as a vertical line called an integral, with the integral value listed under it, as seen in the proton NMR spectrum of benzyl acetate. Each integral value is divided by the smallest integral value to obtain the ratio of the number of protons producing each signal. The ratio reveals the relative number of protons and not...
4.0K
Applications Of NMR In Biology
4.7K
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.
4.7K
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...
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...
1.6K
2D NMR: Overview of Homonuclear Correlation Techniques
776
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...
COSY90 is the standard two-dimensional (2D) COSY experiment that...
776
NMR Spectrometers: Overview
2.5K
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...
2.5K
Nuclear Magnetic Resonance (NMR): Overview
7.8K
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 spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
7.8K


