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From Proteopedia
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== Function == | == Function == | ||
| - | Chaperones bind to the newly synthesized proteins helping them acquire their properly folded 3D structure <ref name="Ellis J"> | + | Chaperones bind to the newly synthesized proteins helping them acquire their properly folded 3D structure <ref name="Ellis J"> 1987.Proteins as Molecular Chaperones. Nature. 5;328(6129):378-9 PMID: 3112578</ref> Besides, chaperones help in targeting the native proteins to their respective organelles <ref name=Deshaies R>Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. 1988.A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature. 332(6167):800-5. PMID:3282178</ref> |
== Disease == | == Disease == | ||
Revision as of 16:31, 9 June 2014
'Chaperones'
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ 1987.Proteins as Molecular Chaperones. Nature. 5;328(6129):378-9 PMID: 3112578
