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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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...
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,...
Mechanisms of Heat Transfer01:14

Mechanisms of Heat Transfer

Heat transfer between the human body and its environment occurs through four main mechanisms: conduction, convection, radiation, and evaporation.
Conduction, accounting for approximately 3% of body heat loss at rest, is the process of exchanging heat between molecules of two materials in direct contact. This can result in both heat loss and gain. For instance, when the body is submerged in water, which conducts heat 20 times more effectively than air, it can either lose or gain significant heat.

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Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
04:45

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

Heat transfer in protein-water interfaces.

Anders Lervik1, Fernando Bresme, Signe Kjelstrup

  • 1Department of Chemistry, Imperial College London, London, UKSW7 2AZ.

Physical Chemistry Chemical Physics : PCCP
|February 4, 2010
PubMed
Summary

This study reveals that protein temperature relaxation can be modeled macroscopically. The protein-water interface significantly influences thermal relaxation, with proteins potentially developing larger internal temperature gradients than water.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Materials Science

Background:

  • Understanding heat transfer in biological systems is crucial for molecular dynamics.
  • Proteins play vital roles in cellular functions, and their thermal properties are key to their activity.

Purpose of the Study:

  • To investigate the temperature relaxation dynamics of structurally diverse proteins (myoglobin, GFP, Ca(2+)-ATPase) in water.
  • To compute thermal conductivity, thermal diffusivity, and protein-water interface thermal conductance.
  • To assess the applicability of macroscopic heat diffusion models to biomolecular systems.

Main Methods:

  • Transient non-equilibrium molecular dynamics simulations were employed.
  • The heat diffusion equation was used to model temperature relaxation.
  • Thermal conductivity, diffusivity, and interface conductance were calculated.

Main Results:

  • Protein temperature relaxation is accurately described by macroscopic models.
  • Protein-water interface thermal conductance is approximately 100-270 MW K(-1) m(-2).
  • Protein thermal conductivity (0.1-0.2 W K(-1) m(-1)) is lower than water's, suggesting internal temperature gradients.
  • Ca(2+)-ATPase exhibits higher thermal diffusivity than myoglobin or GFP.
  • Kapitza length is ~1 nm, highlighting the interface's role.

Conclusions:

  • The protein-water interface is critical for biomolecular thermal relaxation.
  • Proteins can sustain larger internal temperature gradients than their aqueous environment.
  • Macroscopic heat transfer principles are applicable to protein systems.