Biomolecular complex

Multi tool use
Multi tool use

Biomolecular complex, also called macromolecular complex or biomacromolecular complex, is any biological complex made of more than one molecule of protein, RNA, DNA,
[1]lipids, carbohydrates. The interactions between these biomolecules are non-covalent.
[2]
Examples:



  • Protein complexes, some of which are multienzyme complexes: proteasome, DNA polymerase III holoenzyme, RNA polymerase II holoenzyme, symmetric viral capsids, chaperonin complex GroEL-GroES, photosystem I, ATP synthase, ferritin.

  • RNA-protein complexes: ribosome, spliceosome, vault, SnRNP. Such complexes in cell nucleus are called ribonucleoproteins (RNPs).

  • DNA-protein complexes: nucleosome.

  • Protein-lipid complexes: lipoprotein.[3][4]

The biomacromolecular complexes are studied structurally by X-ray crystallography, NMR spectroscopy of proteins, cryo-electron microscopy and successive single particle analysis, and electron tomography.
[5]
The atomic structure models obtained by X-ray crystallography and biomolecular NMR spectroscopy can be docked into the much larger structures of biomolecular complexes obtained by lower resolution techniques like electron microscopy, electron tomography, and small-angle X-ray scattering.
[6]



See also


  • Quaternary structure

  • Multiprotein complex


  • Macromolecular assembly: macromolecular assembly in biology is the same as biomacromolecular complex.


  • Organelle: the broadest definition of "organelle" includes not only membrane bound cellular structures, but also very large biomolecular complexes.

  • Multi-state modeling of biomolecules


References




  1. ^ Kleinjung, Jens; Franca Fraternali (2005-07-01). "POPSCOMP: an automated interaction analysis of biomolecular complexes". Nucleic Acids Research. 33 (suppl 2): W342–W346. doi:10.1093/nar/gki369. ISSN 0305-1048. PMC 1160130. PMID 15980485. Retrieved 2013-11-14..mw-parser-output cite.citationfont-style:inherit.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .citation .cs1-lock-free abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-subscription abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registrationcolor:#555.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted;cursor:help.mw-parser-output .cs1-ws-icon abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center.mw-parser-output code.cs1-codecolor:inherit;background:inherit;border:inherit;padding:inherit.mw-parser-output .cs1-hidden-errordisplay:none;font-size:100%.mw-parser-output .cs1-visible-errorfont-size:100%.mw-parser-output .cs1-maintdisplay:none;color:#33aa33;margin-left:0.3em.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-formatfont-size:95%.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-leftpadding-left:0.2em.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-rightpadding-right:0.2em


  2. ^ Moore, Peter B. (2012). "How Should We Think About the Ribosome?". Annual Review of Biophysics. 41 (1): 1–19. doi:10.1146/annurev-biophys-050511-102314. PMID 22577819.



  3. ^
    Dutta, Shuchismita; Berman, Helen M. (2005-03-01). "Large Macromolecular Complexes in the Protein Data Bank: A Status Report". Structure. 13 (3): 381–388. doi:10.1016/j.str.2005.01.008. ISSN 0969-2126. PMID 15766539. Retrieved 2018-07-11.


  4. ^ Russell, Robert B; Frank Alber; Patrick Aloy; Fred P Davis; Dmitry Korkin; Matthieu Pichaud; Maya Topf; Andrej Sali (June 2004). "A structural perspective on protein–protein interactions". Current Opinion in Structural Biology. 14 (3): 313–324. doi:10.1016/j.sbi.2004.04.006. ISSN 0959-440X. PMID 15193311. Retrieved 2013-04-13.


  5. ^ van Dijk, Aalt D. J.; Rolf Boelens; Alexandre M. J. J. Bonvin (2005). "Data-driven docking for the study of biomolecular complexes". FEBS Journal. 272 (2): 293–312. doi:10.1111/j.1742-4658.2004.04473.x. ISSN 1742-4658.




Further reading



  • .mw-parser-output .smallcapsfont-variant:small-caps
    Berg, J.
    Tymoczko, J. and
    Stryer, L., Biochemistry. (W. H. Freeman and Company, 2002),
    ISBN 0-7167-4955-6



  • Cox, M. and
    Nelson, D. L., Lehninger Principles of Biochemistry. (Palgrave Macmillan, 2004),
    ISBN 0-7167-4339-6








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