Transmembrane protein: Difference between revisions

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A [[Transmembrane|transmembrane]] protein is a protien with [[Hydrophilic|hydrophilic]] and [[Hydrophobic|hydrophobic]] regions which span the&nbsp;[[Lipid bilayer|lipid bilayer]]. These proteins can either be 'single-pass' meaning it crosses the membrane once or 'multipass' and therefore cross the bilayer more than once. [[Transmembrane proteins|Transmembrane proteins]] are usually either single [[Alpha helix|alpha helices]], multiple alpha helices or a [[Beta-sheet|beta sheet]] that has been rolled and is referred to as a beta barrel<ref>Alberts et al (2008) Molecular Biology of the Cell, 5th edition, New York Garland Science, Chapter 10, pages 629-630</ref>.&nbsp;&nbsp;<br>  
A [[Transmembrane|transmembrane]] protein is a protien with [[Hydrophilic|hydrophilic]] and [[Hydrophobic|hydrophobic]] regions which span the&nbsp;[[Lipid bilayer|lipid bilayer]]. These proteins can either be 'single-pass' meaning it crosses the membrane once or 'multipass' and therefore crosses the bilayer more than once. [[Transmembrane proteins|Transmembrane proteins]] are usually either a single [[Alpha helix|alpha helix]], multiple alpha helices or a [[Beta-sheet|beta sheet]] that has been rolled and is referred to as a beta barrel<ref>Alberts et al (2008) Molecular Biology of the Cell, 5th edition, New York Garland Science, Chapter 10, pages 629-630</ref>.&nbsp;&nbsp;<br>  


=== References  ===
=== References  ===


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Revision as of 10:27, 4 December 2015

A transmembrane protein is a protien with hydrophilic and hydrophobic regions which span the lipid bilayer. These proteins can either be 'single-pass' meaning it crosses the membrane once or 'multipass' and therefore crosses the bilayer more than once. Transmembrane proteins are usually either a single alpha helix, multiple alpha helices or a beta sheet that has been rolled and is referred to as a beta barrel[1].  

References

  1. Alberts et al (2008) Molecular Biology of the Cell, 5th edition, New York Garland Science, Chapter 10, pages 629-630