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Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
Noncovalent Attractions in Biomolecules02:35

Noncovalent 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,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent 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,...
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...

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Related Experiment Video

Updated: Jun 3, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

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

Published on: April 28, 2022

Hydrodynamic effects in proteins.

Piotr Szymczak1, Marek Cieplak

  • 1Institute of Theoretical Physics, Faculty of Physics, University of Warsaw, Hoża 69, 00-681 Warsaw, Poland. piotr.szymczak@fuw.edu.pl

Journal of Physics. Condensed Matter : an Institute of Physics Journal
|March 17, 2011
PubMed
Summary
This summary is machine-generated.

This review covers how fluid flow affects protein structures, focusing on shear-induced unfolding and solvent interactions during conformational changes. Understanding these protein dynamics is crucial for molecular biology.

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Last Updated: Jun 3, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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Published on: April 28, 2022

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

  • Biophysics
  • Molecular Biology
  • Computational Chemistry

Background:

  • Proteins undergo conformational changes influenced by their environment.
  • Fluid dynamics can significantly impact protein structure and function.
  • Hydrodynamic interactions play a key role in molecular processes.

Purpose of the Study:

  • To review experimental and numerical findings on flow-induced effects in proteins.
  • To highlight the mechanisms of shear-induced protein unfolding.
  • To elucidate the role of solvent-mediated hydrodynamic interactions in protein conformational transitions.

Main Methods:

  • Review of experimental studies on protein behavior under flow.
  • Analysis of numerical simulations investigating protein dynamics.
  • Examination of theoretical models for hydrodynamic interactions.

Main Results:

  • Shear stress can induce unfolding in protein structures.
  • Solvent interactions significantly mediate hydrodynamic forces.
  • These forces are critical for conformational transitions in proteins.

Conclusions:

  • Flow-induced effects are a significant factor in protein conformational dynamics.
  • Shear-induced unfolding is a key phenomenon driven by fluid forces.
  • Solvent hydrodynamics are essential for understanding protein behavior under stress.