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Related Concept Videos

Hydrogen Bonds00:26

Hydrogen Bonds

Hydrogen BondsHydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.Hydrogen Bonds Control the World!Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are...
Hydrogen Bonds01:04

Hydrogen Bonds

A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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 cytoskeletal...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...

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Updated: Jun 24, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Hydrogen bonds in membrane proteins.

Sheh-Yi Sheu1, Edward W Schlag, Heinrich L Selzle

  • 1Department of Life Sciences and Institute of Biomedical Informatics, National Yang-Ming University, Taipei 112, Taiwan. sysheu@ym.edu.tw

The Journal of Physical Chemistry. B
|April 10, 2009
PubMed
Summary
This summary is machine-generated.

Protein hydrogen bonds break and reform rapidly. Water environments lower binding energy and increase rates, while lipids offer a different balance of energy and entropy for faster protein dynamics.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Protein Dynamics

Background:

  • Protein structures rely on hydrogen bonds, which dynamically rupture and reform on picosecond timescales.
  • Environmental factors, particularly water, significantly influence hydrogen bond dynamics and protein activity.
  • Previous simulations highlighted long-range solvent effects on hydrogen bond energy and entropy.

Purpose of the Study:

  • To investigate the impact of lipid environments on protein hydrogen bond dynamics.
  • To compare the effects of water and lipid environments on hydrogen bond energy, entropy, and rupture rates.
  • To understand how solvent effects influence protein reactivity and dynamics in different biological contexts.

Main Methods:

  • Molecular dynamics simulations were employed to model hydrogen bonds within lipid environments.
  • Analysis focused on energy contributions, entropic changes, and kinetic rate constants.
  • Comparison with existing data for hydrogen bonds in water and isolated molecules.

Main Results:

  • Lipid environments reduce hydrogen bond energy compared to isolated molecules, but less so than water.
  • Unlike water, lipid environments do not impose an entropic penalty for hydrogen bond rupture.
  • The reduced entropic penalty in lipids leads to faster hydrogen bond rupture rates than in water, despite higher energy.

Conclusions:

  • Solvent environments profoundly impact hydrogen bond thermodynamics and kinetics, affecting protein dynamics.
  • Lipid environments facilitate faster protein hydrogen bond dynamics compared to aqueous environments due to entropic factors.
  • Accurate modeling of long-range solvent effects on entropy is crucial for predicting protein mobility and reactivity.