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Cytochrome c
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=== Dipole moment === The dipole moment has an important role in orienting proteins to the proper directions and enhancing their abilities to bind to other molecules.<ref>{{Cite journal |vauthors=Koppenol WH, Margoliash E |date=April 1982 |title=The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications |journal=The Journal of Biological Chemistry |volume=257 |issue=8 |pages=4426β37 |doi=10.1016/S0021-9258(18)34740-9 |pmid=6279635 |doi-access=free}}</ref><ref name="Koppenol_1982">{{Cite journal |vauthors=Koppenol WH, Rush JD, Mills JD, Margoliash E |date=July 1991 |title=The dipole moment of cytochrome c |journal=[[Molecular Biology and Evolution]] |volume=8 |issue=4 |pages=545β58 |doi=10.1093/oxfordjournals.molbev.a040659 |pmid=1656165 |doi-access=free}}</ref> The dipole moment of cytochrome c results from a cluster of negatively charged amino acid side chains at the "back" of the enzyme.<ref name="Koppenol_1982" /> Despite variations in the number of bound heme groups and variations in sequence, the dipole moment of vertebrate cytochromes c is remarkably conserved. For example, vertebrate cytochromes c all have a dipole moment of approximately 320 [[debye]] while cytochromes c of plants and insects have a dipole moment of approximately 340 debye.<ref name="Koppenol_1982" />
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