Related Experiment Video
Updated: Aug 6, 2026
09:48
In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
Published on: February 15, 2016
Low-frequency collective modes in dry and hydrated proteins
M C Bellissent-Funel1, J Teixeira, S H Chen
1Laboratoire Léon Brillouin, C.E.N. Saclay, Gif-sur-Yvette, France.
Biophysical Journal
|October 1, 1989
Summary
Researchers detected low-frequency collective modes in deuterated proteins using neutron scattering. These findings suggest short-lived excitations moving at high velocities within protein structures and associated water.
Area of Science:
- Biophysics
- Neutron Scattering
- Protein Dynamics
Background:
- Understanding protein dynamics is crucial for deciphering biological functions.
- Collective modes offer insights into large-scale molecular motions.
Purpose of the Study:
- To investigate low-frequency collective modes in proteins using neutron scattering.
- To characterize the nature and velocity of these dynamic excitations.
Main Methods:
- Neutron scattering experiments were performed on a fully in vivo deuterated protein.
- Analysis focused on observing low-frequency collective modes.
Main Results:
- Brillouin-like low-frequency collective modes were observed.
- These modes exhibit velocities ranging from 2,000 to 4,000 m/s.
- The excitations are tentatively linked to protein secondary structures and associated water patches.
Conclusions:
- The study reveals the presence of high-velocity collective excitations in proteins.
- These findings provide new insights into the dynamic behavior of proteins and associated water molecules.
Related Concept Videos
01:22Protein Folding
Overview
02:21Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
01:23IR Spectrum Peak Broadening: Hydrogen Bonding
The vibrational frequency of a bond is directly proportional to its bond strength. As a result, stronger bonds vibrate at higher frequencies, while weaker bonds vibrate at lower frequencies. The stretching vibration of the strong O–H bond in alcohols and phenols (very dilute solution or gas phase) appears as a sharp peak at 3600–3650 cm−1.
However, the extent of hydrogen bonding influences the observed stretching frequency and band broadening. Intermolecular or intramolecular hydrogen bonding...
However, the extent of hydrogen bonding influences the observed stretching frequency and band broadening. Intermolecular or intramolecular hydrogen bonding...
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...
02:21Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
00:55Fibrous Proteins
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...