Related Experiment Video
Updated: May 20, 2026
10:07
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
Published on: August 26, 2025
Wide-line NMR and protein hydration
1Research Institute for Solid State Physics and Optics, Hungarian Academy of Sciences, Budapest, Hungary.
Methods in Molecular Biology (Clifton, N.J.)
|July 5, 2012
Summary
This chapter introduces wide-line Nuclear Magnetic Resonance (NMR) spectrometry basics, covering theory, data interpretation, and practical experimental design. It provides essential guidance for novices, including solvent selection and data validation, with protein case studies.
Area of Science:
- Analytical Chemistry
- Biophysical Chemistry
- Spectroscopy
Background:
- Wide-line Nuclear Magnetic Resonance (NMR) spectrometry is a powerful technique for studying molecular dynamics and structure.
- Understanding the fundamental principles and experimental design is crucial for effective data acquisition and interpretation.
- Novice researchers often face challenges in selecting appropriate solvents and validating data quality.
Purpose of the Study:
- To provide a comprehensive introduction to the basics of wide-line NMR spectrometry.
- To guide readers through theoretical and experimental aspects, data interpretation models, and practical considerations.
- To offer insights into solvent selection and data quality assessment for improved experimental outcomes.
Main Methods:
- Detailed explanation of basic theoretical and experimental Nuclear Magnetic Resonance (NMR) elements.
- Introduction to models and theories for interpreting measured wide-line NMR data.
- Description of measurement and evaluation variants with practical advice for novice users.
Main Results:
- The chapter defines wide-line NMR spectrometry and outlines measurement and evaluation strategies.
- It offers specific advice on solvent selection, a critical but often overlooked parameter.
- The importance of data validation beyond statistical confidence is highlighted, with examples from globular and intrinsically disordered proteins.
Conclusions:
- This chapter equips readers with foundational knowledge for wide-line NMR spectrometry.
- It emphasizes practical aspects, including experimental design, data interpretation, and quality control.
- The presented information and case studies serve as a valuable resource for researchers new to the technique.
Related Concept Videos
01:15¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
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.
01:19NMR 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...
01:162D NMR: Overview of Homonuclear Correlation Techniques
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...
01:02¹H NMR: Interpreting Distorted and Overlapping Signals
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
01:10¹H NMR of Labile Protons: Temporal Resolution
Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
01:07Proton (¹H) NMR: Chemical Shift
Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei in a...
Absorption signals of all the protium nuclei in a...