In chemistry, an oligomer (\ə-ˈli-gə-mər\, ολιγος, or oligos, is Greek for "a few") is a molecular complex that consists of a few monomer units, in contrast to a polymer that, at least in principle, consists of a nearly unlimited number of monomers.Dimers, trimers, and tetramers are, for instance, oligomers respectively composed of two, three and four monomers.
In the context of biochemistry, an oligomer is usually referred to a macromolecular complex formed by non-covalent bonding of few macromolecules like proteins or nucleic acids. In this sense, a homo-oligomer would be formed by few identical molecules and by contrast, a hetero-oligomer would be made of three different macromolecules. Collagen is an example of homo-oligomeric protein that is composed of three identical protein chains.
Many oils are oligomeric, such as liquid paraffin. Plasticizers are oligomeric esters widely used to soften thermoplastics such as PVC. They may be made from monomers by linking them together, or by separation from the higher fractions of crude oil. Polybutene is an oligomeric oil used to make putty. Greek prefixes are often used to designate the number of monomer units in the oligomer, for example a tetramer being composed of four units and a hexamer of six.
In biochemistry, the term oligonucleotide - or, informally, "oligo" - is used for short, single-stranded nucleic acid fragments, such as DNA or RNA, or similar fragments of analogs of nucleic acids such as peptide nucleic acid or Morpholinos. Such oligos are used in hybridization experiments (bound to glass slides or nylon membranes), as probes for in situ hybridization or in antisense experiments such as gene knockdowns.[citation needed] It can also refer to a protein complex made of two or more subunits. In this case, a complex made of several different protein subunits is called a hetero-oligomer or heteromer. When only one type of protein subunit is used in the complex, it is called a homo-oligomer or homomer.
Oligomerization is a chemical process that converts monomers to macromolecular complexes through a finite degree of polymerization. The actual figure for degree of polymerization is a matter of debate, often a value between 10 and 100.[citation needed]
When an oligomer forms as a result of chain transfer the oligomer is called a telomer and the process telomerization. A telomere is a region of highly repetitive DNA at the end of a linear chromosome.

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oligomerization - The Free Dictionary
o·lig·o·mer ( -l g -m r). n. A polymer that consists of two, three, or four monomers. o ·lig o·mer ic (-m r k) adj. o·lig o·mer i·za tion n. oligomer [ɒˈlɪgəmə]. n.
Protein oligomerization: How and why
Review. Protein Oligomerization: How and why. Mayssam H. Ali and Barbara Imperiali*. Department of Chemistry, Massachusetts Institute of Technology, ...
Oligomer - Wikipedia, the free encyclopedia
Oligomerization: The process of converting a monomer or a mixture of monomers ... Note: An Oligomerization by chain reaction carried out in the presence of a ...
IUPAC Gold Book - oligomerization
The process of converting a monomer or a mixture of monomers into an oligomer. An Oligomerization by chain reaction carried out in the presence of a large ...
GO:0051259 protein oligomerization
ID, GO:0051259. Name, protein Oligomerization. Ontology, Biological Process. Definition, The process of creating protein oligomers, compounds composed of a ...
Oligomerization is a general mechanism for the activation of ...
J Biol Chem. 2003 May 9;278(19):16466-9. Epub 2003 Mar 13. Oligomerization is a general mechanism for the activation of apoptosis initiator and inflammatory ...
The detection and quantitation of protein oligomerization.
Adv Exp Med Biol. 2012;747:19-41. doi: 10.1007/978-1-4614-3229-6_2. The detection and quantitation of protein Oligomerization. Gell DA, Grant RP, Mackay JP ...
oligomerization - Wiktionary
English[edit]. Noun[edit]. Oligomerization (plural Oligomerizations). (chemistry) The formation of an oligomer from a monomer ...
Protein oligomerization: How and why - ScienceDirect
A large fraction of cellular proteins are oligomeric. Protein Oligomerization may often be an advantageous feature from the perspective of protein evolution and.
Oligomerization - Axens
Axens Oligomerization technologies rely on strong expertise accumulated over 50 years in order to provide the most appropriate solutions to achieve high ...
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Oligomerization in science
Amyloid-beta oligomerization in Alzheimer dementia versus high ...
Dec 7, 2012 ... Amyloid-beta Oligomerization in Alzheimer dementia versus high-pathology controls. Thomas J. Esparza BS1,; Hanzhi Zhao BS1,; John R.
A Structural Basis for IκB Kinase 2 Activation Via Oligomerization ...
Reversible Oligomerization of hIKK2 dimers is observed in solution. ... Academic Editor: Gregory A. Petsko, Brandeis University, United States of America.
Fibril-mediated oligomerization of pilin-derived protein nanotubes
Jul 5, 2013 ... 1 Department of Chemistry, York University, Toronto, ON M3J1P3, ... The optimal initiator for the Oligomerization of ΔK122 in solution was ...
Deadly folding mistake: Molecular mechanism of prion protein - Phys
Aug 16, 2013 ... Kai Schlepckow and Harald Schwalbe at the Goethe University ... Certain regions of the protein stiffen as the Oligomerization proceeds.
Role of Oligomerization in Discoidin Domain Receptors-Collagen ...
2008, Doctor of Philosophy, Ohio State University, Biophysics. ... We found that both DDR1 and DDR2 ECD require Oligomerization for binding to collagen type I.
Kaede for Detection of Protein Oligomerization
Feb 21, 2013 ... Kaede for Detection of Protein Oligomerization ... Office in association with Oxford University Press on behalf of CSPB and IPPE, SIBS, CAS.
Orally Administrated Cinnamon Extract Reduces β-Amyloid ...
Jan 28, 2011 ... Affiliation: Department of Zoology, Tel Aviv University, Tel Aviv, Israel ... of common edible elements to modulate Aβ Oligomerization remains an ...
Hsp70 Oligomerization Is Mediated by an Interaction between the ...
Affiliation: Department of Biotechnology and Biosciences, University of Milano- Bicocca, ... Oligomerization in the heat shock protein (Hsp) 70 family has been ...
Self-Oligomerization Is Essential for Enhanced Immunological ...
Affiliation: Institute of Biology and Medical Sciences, Soochow University, Suzhou , ... When rCRT/18-412 is fractionated into oligomers and monomers by gel ...
Oligomerization of DHHC Protein S-Acyltransferases
Aug 2, 2013 ... From the Department of Molecular Medicine, Cornell University ... Background: Oligomerization of DHHC palmitoyltransferases has been ...
Books on the term Oligomerization
Oligomerization in Health and Disease
Oligomerization in Health and Disease
This special volume of Progress in Molecular Biology and Translational Science focuses on Oligomerization in health and disease.
Oligomerization and Allosteric Modulation in G-Protein Coupled ...
Oligomerization and Allosteric Modulation in G-Protein Coupled ...
In this thematic volume of Progress in Molecular Biology and Translational Science, researchers reflect on recent developments and research surrounding G protein-coupled receptors.
Synthesis and Characterization of Oligomers
Synthesis and Characterization of Oligomers
Constantin V. Uglea, Ioan I. Negulescu, 1991
This book provides an excellent introduction to the fundamentals of oligomer chemistry.
Inorganic Reactions and Methods, Oligomerization and ...
Inorganic Reactions and Methods, Oligomerization and ...
J. J. Zuckerman, A. P. Hagen, 2009
The work is indexed in a unique way by a structured system which maximizes its usefulness to the reader. It augments the organization of the work by providing additional routes of access for specific compounds, reactions and other topics.
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Radical mechanisms of methyl vinyl ketone oligomerization through ...
Deadly folding mistake: Molecular mechanism of prion protein oligomerization at atomic resolution
(Phys.org) —Mad cow disease and its cousin Creutzfeld-Jakob disease cause fatal spongy changes in brain tissue. Today, we know that these diseases are caused by prions, proteins that are folded incorrectly. A team of German researchers have now been able to follow how the diseased proteins aggregate ...
Oligomerization of DHHC Protein S-Acyltransferases
JN | Full text | Fibril-mediated oligomerization of pilin-derived protein nanotubes
Self-assembling protein nanotubes (PNTs) are an intriguing alternative to carbon nanotubes for applications in bionanotechnology, in part due to greater inherent biocompatibility. The type IV pilus of the gram negative bacteria Pseudomonas aeruginosa is a protein-based fibre composed of a single subunit, the type IV pilin. Engineered pilin monomers from P. aeruginosa strain K122-4 (ΔK122) have been shown to oligomerize into PNTs both in solution and at surfaces. In order to fully exploit PNTs in bionanotechonological settings, an in-depth understanding of their assembly, physical characteristics and robustness, both in solution and when constrained to surfaces, is required.
Molecules | Free Full-Text | Oligomerization of 10,16-Dihydroxyhexadecanoic Acid and Methyl 10,16-Dihydroxyhexadecanoate Catalyzed by Lipases
Molecules, an international, peer-reviewed Open Access journal.
JCI - C3 glomerulopathy–associated CFHR1 mutation alters FHR oligomerization and complement regulation
"SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subce" by Gloria Salazar, Juan M. Falcon-Perez et al.
Non-covalent and covalent homo-Oligomerization of membrane proteins regulates their subcellular localization and function. Here, we described a novel Oligomerization mechanism affecting solute carrier family 30 member 3/zinc transporter 3 (SLC30A3/ZnT3). Oligomerization was mediated by intermolecular covalent dityrosine bonds. Using mutagenized ZnT3 expressed in PC12 cells, we identified two critical tyrosine residues necessary for dityrosine-mediated ZnT3 Oligomerization. ZnT3 carrying the Y372F mutation prevented ZnT3 Oligomerization, decreased ZnT3 targeting to synaptic-like microvesicles (SLMVs), and decreased resistance to zinc toxicity. Strikingly, ZnT3 harboring the Y357F mutation behaved as a ‘‘gain-of-function’’ mutant as it displayed increased ZnT3 Oligomerization, targeting to SLMVs, and increased resistance to zinc toxicity. Single and double tyrosine ZnT3 mutants indicate that the predominant dimeric species is formed between tyrosine 357 and 372. ZnT3 tyrosine dimerization was detected under normal conditions and it was enhanced by oxidative stress. Covalent species were also detected in other SLC30A zinc transporters localized in different subcellular compartments. These results indicate that covalent tyrosine dimerization of a SLC30A family member modulates its subcellular localization and zinc transport capacity. We propose that dityrosine-dependent membrane protein Oligomerization may regulate the function of diverse membrane protein in normal and disease states.
PML-RARα and Its Phosphorylation Regulate PML Oligomerization and HIPK2 Stability
We’ve thus demonstrated that Bax and Bak oligomerization at | PKC Pathway
Posted on August 25, 2013 by pkcp2456.
Interference with RUNX1/ETO Leukemogenic Function by Cell-Penetrating Peptides Targeting the NHR2 Oligomerization Domain
BioMed Research International (formerly titled Journal of Biomedicine and Biotechnology) is a peer-reviewed, open access journal that publishes original research articles as well as review articles in several areas of life sciences. The journal’s Editorial Board is divided into the 55 subject areas included within the journal’s scope.