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Integral membrane protein
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==Function== IMPs include [[membrane transport protein|transporters]], linkers, [[Ion channel|channels]], [[receptor (biochemistry)|receptors]], [[enzyme]]s, structural membrane-anchoring domains, proteins involved in accumulation and [[transduction (biophysics)|transduction]] of [[energy]], and proteins responsible for [[cell adhesion]]. Classification of transporters can be found in [[Transporter Classification Database]].<ref name="pmid19022853">{{cite journal |vauthors=Saier MH, Yen MR, Noto K, Tamang DG, Elkan C |title=The Transporter Classification Database: recent advances |journal=Nucleic Acids Res. |volume=37 |issue=Database issue |pages=D274β8 |date=January 2009 |pmid=19022853 |pmc=2686586 |doi=10.1093/nar/gkn862 |url=}}</ref> As an example of the relationship between the IMP (in this case the bacterial phototrapping pigment, bacteriorhodopsin) and the membrane formed by the phospholipid bilayer is illustrated below. In this case the integral membrane protein spans the phospholipid bilayer seven times. The part of the protein that is embedded in the hydrophobic regions of the bilayer are alpha helical and composed of predominantly hydrophobic amino acids. The C terminal end of the protein is in the cytosol while the N terminal region is in the outside of the cell. A membrane that contains this particular protein is able to function in photosynthesis.<ref>{{cite web |url=http://academic.brooklyn.cuny.edu/biology/bio4fv/page/integra.htm |website=academic.brooklyn.cuny.edu |title=Integral membrane proteins |access-date=29 January 2015 |archive-url=https://web.archive.org/web/20150201184055/http://academic.brooklyn.cuny.edu/biology/bio4fv/page/integra.htm |archive-date=1 February 2015 |url-status=dead }}</ref>
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