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Related Concept Videos

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
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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.
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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...
Hydrogen Bonds00:26

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Hydrogen 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.
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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...
Mechanisms of Membrane-bending01:15

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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Hydrogen bond dynamics in membrane protein function.

Ana-Nicoleta Bondar1, Stephen H White

  • 1Theoretical Molecular Biophysics, Freie Universität Berlin, Department of Physics, Arnimallee 14, 14195 Berlin, Germany. nbondar@zedat.fu-berlin.de

Biochimica Et Biophysica Acta
|December 20, 2011
PubMed
Summary
This summary is machine-generated.

Dynamical hydrogen bonds in membrane proteins regulate function by enabling long-distance coupling. These bonds stabilize protein structures and facilitate rapid communication within the protein and with the lipid membrane.

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Published on: April 2, 2015

Area of Science:

  • Biophysics
  • Structural Biology
  • Membrane Protein Dynamics

Background:

  • Membrane protein function is intrinsically linked to their surrounding lipid environment.
  • Conformational dynamics are crucial for the activity of membrane proteins.
  • Inter-helical hydrogen bonding plays a key role in protein structure and flexibility.

Purpose of the Study:

  • To review the role of dynamical hydrogen bonds in membrane protein function.
  • To highlight mechanisms of long-distance coupling mediated by hydrogen bonds.
  • To discuss the contribution of hydrogen bonds to protein stability and signal propagation.

Main Methods:

  • Review of specific examples from scientific literature.
  • Analysis of structural and dynamic data related to membrane proteins.
  • Focus on hydrogen bonding patterns and their functional implications.

Main Results:

  • Dynamical hydrogen bonds provide efficient long-distance intra-protein coupling.
  • These bonds facilitate effective protein-lipid coupling, influencing protein function.
  • Hydrogen bonding contributes to the stabilization of distinct protein conformational substates.
  • Rapid propagation of structural perturbations is mediated by these dynamic interactions.

Conclusions:

  • Dynamical hydrogen bonds are essential for the functional adaptability of membrane proteins.
  • These bonds serve as a critical link between protein structure, dynamics, and lipid interactions.
  • Understanding these mechanisms is key to deciphering membrane protein behavior and function.