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Related Concept Videos

Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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...
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...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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MAPS: an interactive web server for membrane annotation of transmembrane protein structures.

Jitender Cheema1, Gautam Basu

  • 1Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India. jitender.cheema@bbsrc.ac.uk

Indian Journal of Biochemistry & Biophysics
|June 21, 2011
PubMed
Summary

This study annotates the membrane position for transmembrane (TM) proteins using a novel energy function. A web server, MAPS, is introduced for interactive analysis of protein-membrane orientations.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Transmembrane (TM) proteins are crucial for cellular functions, and their membrane positioning is vital.
  • Existing protein data bank (PDB) structures lack explicit information on the membrane environment of TM proteins.

Purpose of the Study:

  • To develop a computational method for predicting the membrane bilayer position of TM proteins.
  • To create a user-friendly web server for analyzing TM protein-membrane interactions.

Main Methods:

  • Utilized a hydrophobic lipid-protein mismatch energy function.
  • Incorporated a flexible lipid/water boundary to simulate the membrane environment.
  • Applied the method to representative TM proteins from the PDB.

Main Results:

  • Successfully annotated the lipid bilayer positions for various TM proteins.
  • Developed the Membrane Annotation of Protein Structures (MAPS) web server.
  • MAPS allows interactive analysis of protein-membrane orientations with adjustable parameters.

Conclusions:

  • The developed method and MAPS web server provide valuable tools for understanding TM protein structure and function within the membrane.
  • Accurate annotation of membrane positioning enhances the study of TM protein behavior and interactions.