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Related Concept Videos

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,...
Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
Cohesion01:07

Cohesion

Cohesion is the attraction between molecules of the same type, such as water molecules. Water molecules have an overall neutral charge but are polar molecule. An oxygen atom in one water molecule has a partial negative charge that can bind to a hydrogen atom with a partial positive charge in a second water molecule, forming a hydrogen bond. Each water molecule can form up to four hydrogen bonds with other water molecules. Hydrogen bonds are responsible for water's cohesive nature.
On a surface,...
Protein Folding01:22

Protein Folding

Overview
Intermolecular Forces03:13

Intermolecular Forces

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 bonds, and dispersion...

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Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
09:14

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding

Published on: August 22, 2016

Protein crowding affects hydration structure and dynamics.

Ryuhei Harada1, Yuji Sugita, Michael Feig

  • 1RIKEN Advanced Institute for Computational Science, 7-1-26 minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047 Japan.

Journal of the American Chemical Society
|February 23, 2012
PubMed
Summary
This summary is machine-generated.

Protein crowding significantly alters water structure and dynamics, reducing diffusion and dielectric constants. These findings offer insights into cellular environments and biomolecular stability.

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Published on: April 28, 2022

Area of Science:

  • Biophysics
  • Computational Chemistry
  • Structural Biology

Background:

  • Cellular environments are highly crowded with macromolecules.
  • Understanding macromolecular crowding effects on water is crucial for biological processes.

Purpose of the Study:

  • To investigate the impact of protein crowding on water structure and dynamics.
  • To analyze changes in hydration, diffusion, and dielectric properties under crowded conditions.

Main Methods:

  • Explicit solvent molecular dynamics simulations of protein G and protein G/villin systems.
  • Analysis of radial distribution functions, hydration sites, and tetrahedral coordination.
  • Measurement of self-diffusion rates and dielectric constants at varying protein concentrations.

Main Results:

  • Water structure is altered beyond the first solvation shell in crowded conditions.
  • Diffusion rates and dielectric constants decrease linearly with increasing protein concentration.
  • Water molecules exhibit constrained dynamics in highly crowded environments.

Conclusions:

  • Protein crowding significantly impacts water's structural and dynamic properties.
  • Reduced water dynamics have implications for cellular hydrodynamics.
  • Lowered dielectric constants affect biomolecular stability in crowded cellular milieus.
  • Provides a model for simulating solvation in cellular environments.