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Related Concept Videos

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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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.
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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...
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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
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Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

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Published on: April 20, 2015

Membrane protein structure: prediction versus reality.

Arne Elofsson1, Gunnar von Heijne

  • 1Center for Biomembrane Research, Stockholm Bioinformatics Center, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden. arne@bioinfo.se

Annual Review of Biochemistry
|June 21, 2007
PubMed
Summary

Theoretical structure prediction algorithms are crucial for membrane protein biochemistry due to limited structural data. This study evaluates current methods, identifying predictable features and future expectations for these important computational tools.

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Structural Biology

Background:

  • High-resolution structural data for membrane proteins remain scarce.
  • Theoretical structure prediction algorithms are vital for advancing membrane protein research.
  • Understanding the capabilities and limitations of these algorithms is essential.

Purpose of the Study:

  • To evaluate the performance of current theoretical structure prediction algorithms for membrane proteins.
  • To identify which structural features can be reliably predicted.
  • To forecast future advancements in membrane protein structure prediction.

Main Methods:

  • Review and analysis of existing theoretical structure prediction algorithms.
  • Comparative assessment of prediction accuracy for various structural features.
  • Discussion of current limitations and future trends in the field.

Main Results:

  • Current algorithms show varying degrees of success in predicting membrane protein structures.
  • Specific structural features are more amenable to prediction than others.
  • The field is rapidly evolving with anticipated improvements in accuracy and scope.

Conclusions:

  • Theoretical structure prediction is indispensable for membrane protein biochemistry.
  • Further development is needed to enhance prediction accuracy and reliability.
  • Future research will likely yield more comprehensive and precise structural models.