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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Intermolecular Forces03:13

Intermolecular Forces

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Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen...
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Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Membrane Domains01:18

Membrane Domains

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
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Aquaporins01:25

Aquaporins

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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.
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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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.
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Related Experiment Video

Updated: Apr 5, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Dipolar Nanodomains in Protein Hydration Shells.

Daniel R Martin, Dmitry V Matyushov

    The Journal of Physical Chemistry Letters
    |August 12, 2015
    PubMed
    Summary

    Water

    Area of Science:

    • Biophysics
    • Physical Chemistry
    • Materials Science

    Background:

    • Bulk water's hydrogen bond network is altered at protein interfaces.
    • Local electric fields create frustrated dipolar domains with unique properties.

    Purpose of the Study:

    • Investigate the dipolar susceptibility of lysozyme hydration shells.
    • Explore water dynamics and structure at the protein-water interface across temperatures.

    Main Methods:

    • Molecular dynamics simulations were employed.
    • Simulations covered a temperature range of 140–300 K.

    Main Results:

    • Dipolar susceptibility exhibits a broad maximum with temperature, shifting with frequency.
    • Observed phenomena resemble bulk relaxor ferroelectrics, indicating dipolar nanodomain formation.
    Keywords:
    dipolar nanodomainsprotein dynamicsprotein hydrationrelaxor ferroelectrics

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  • Nanodomains (12–15 Å) show slower dynamics than bulk water and freeze into a glass below 160 K.

    • Conclusions:

    • Protein hydration shells exhibit relaxor ferroelectric-like behavior.
    • Water dynamics at the interface are distinct from bulk water, forming glassy states.
    • Findings suggest novel structure and dynamics at the protein-water interface.