Related Experiment Video
Updated: Jun 16, 2026
08:48
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Water and backbone dynamics in a hydrated protein.
Galina Diakova1, Yanina A Goddard, Jean-Pierre Korb
1Chemistry Department, University of Virginia, Charlottesville, Virginia, USA.
Biophysical Journal
|January 21, 2010
Summary
Rotational immobilization of proteins reveals consistent internal dynamics over a wide frequency range. Water molecule dynamics significantly contribute to protein spin-lattice relaxation, influencing local dielectric properties.
Area of Science:
- Biophysics
- Structural Biology
- Spectroscopy
Background:
- Protein dynamics are crucial for function and can be studied using magnetic relaxation dispersion (MRD) spectroscopy.
- Understanding internal peptide and water molecule dynamics requires broad frequency range measurements.
Purpose of the Study:
- To extend magnetic field dependence measurements of proton spin-lattice relaxation rates for proteins.
- To characterize the role of water molecules in protein relaxation dynamics.
Main Methods:
- Magnetic relaxation dispersion (MRD) spectroscopy was used to measure proton spin-lattice relaxation rates.
- Measurements were extended to cover a magnetic field range from 0.01 to 300 MHz.
- Deuterated water ((2)H(2)O) was used to differentiate contributions from protein and water protons.
Main Results:
- Protein dynamics influencing relaxation were preserved over 4.5 decades in frequency, following a power law.
- Water protons contribute significantly to spin-lattice relaxation in hydrated proteins within a specific frequency range.
- Water molecule dynamics in the tens of nanoseconds range were observed to affect protein relaxation.
Conclusions:
- Protein structural fluctuations causing relaxation are remarkably constant over wide frequency and length scales.
- Confined water molecule dynamics play a key role in the relaxation processes of hydrated proteins.
- Observed water dynamics suggest frequency-dependent local dielectric properties relevant to protein function.
Related Concept Videos
01:22Protein Folding
Overview
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:19Protein Dynamics in Living Cells
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
01:25Aquaporins
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
02:15Protein and Protein Structure
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
A protein's shape is critical to its function. For example, an enzyme can...
02:35Noncovalent Attractions in Biomolecules
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...