Oligomeric proteins

James, J. R., Oliveira, M. I., Carmo, A. M., Iaboni, A. and Davis, S. J. (2006). A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nat. Methods 3, 1001-6. 

Once in the ER lumen, proteins oligomerize and fold. Proper folding in most cases is facilitated by various isomerases and chaperones resident in the ER. Complex mechanisms exist within the ER to ensure that proteins... 

Burcham, P. C. and Pyke, S. M. (2006). Hydralazine inhibits rapid acrolein-induced protein oligomerization Role of aldehyde scavengers and adduct trapping in cross-link blocking and cytoprotection. Mol. Pharm. 69,1056-1065. 

Burkhard, P., Meier, M., and Lustig, A. (2000b). Design of a minimal protein oligomerization domain by a structural approach. Prot. Sci. 9, 2294—2301. 

Bitan, G Lomakin, A. and Teplow, D. B. (2001) Amyloid beta-protein oligomerization prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35176-35184. 

Mattinen, M.L., Heilman, M., Permi, P., Autio, K., Kalkkinen, N., Buchert, J. 2006. Effect of protein structure on laccase-catalysed protein oligomerization. J Agric Food Chem 54 8883-8890. 

Cellular and viral IL-lOs and IFN-7 form intercalated dimers (Fig. 2). The intercalated dimer is formed from the first four secondary structural elements from one chain (A-D) and the final two (E and F) from the other. The intertwined dimer fold observed for IFN-7, IL-10, and many other protein structures, is proposed to be an evolutionary mechanism of protein oligomerization referred to as 3D domain swapping (Bennett et at., 1995). This theory suggests IFN-7 and lL-10 evolved from a monomeric protein by exchanging structural domains (a-helices E and E) with another monomer to create the dimer. This hypothesis is strengthened by the discovery of the monomeric IL-lOFMs, lL-19, IL-20, and IL-22. In fact, the close relationship between the intertwined dimeric IFN-7 and monomeric type 1 IFNs was clearly identified when the first structure of IEN-7 was completed in 1991 (Ealick et at, 1991). 

Tahiri-Alaoui A, Gill AC, Disterer P et al (2004) Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant implications for disease susceptibility to Creutzfeldt-Jakob disease. J Biol Chem 279 31390-31397... 

Hurtley, S. M., and Helenius, A. (1989). Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307. 

Stott, K, Blackburn, J.M., Butler, P.J.G., and Perutz, M. (1995). Incorporation of glutamine repeats makes protein oligomerize implications for neurodegenerative diseases. Proc. Natl. Acad. Sci. U.S.A. 92, 6509-6513. 

Furthermore, three well-defined domains have been identified in FAAH i) a transmembrane domain at the N-terminus which directs protein oligomerization, ii) a serine- and glycine-rich domain, and iii) a proline-rich domain. 

The anthozoan protein amajCFP as well as its mutant amajCFP-II (see table 5) form tetramers as judged by semi-native gel-electrophoresis [55]. For the anthozoan CFPs protein oligomerization and aggregation needs to be investigated. 

Westerlund JA, Weisgraber KH. Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization. J Biol Chem 1993 268 15745-15750. 

Bitan G, Vollers SS, Teplow DB (2003b) Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization. J Biol Chem 278 34882-34889 Blake C, Serpell L (1996) Synchrotron X-ray smdies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet heUx. Structure 4 989-998... 

In studies of the dynamics of protein oligomerization in the context of investigations exploring amyloidoses, i.e. diseases including Alzheimer s disease, ruthe-nium(II) complexes are used [52, 55]. To this end, tris(2,2 -bipyridyl)dichloro-ruthenium(II), Ru(II)bpy3Cl2 (see Chart 8.8), and ammonium persulfate, (NH4)2S20g, are homogeneously dispersed in an aqueous protein solution. 

AFM images provide structural information on proteins and their interactions with other proteins or other molecules such asDNA. From visual inspection of the data, conformational properties of proteins can often be directly derived, as shown for example in Fig. 5a [9]. Quantitative statistical analyses allow for the extraction of further information on protein states and interactions. From the measured volume of particles in the images, their molecular mass can be calculated [10]. This calculation is based on an empirically derived linear relationship obtained with calibratirm proteins with a range of known molecular weights. From the molecular mass of the protein molecules and complexes, information can be derived on protein oligomeric states, protein-protein interactions, and complex stoichiometries. Single molecule resolution coupled with the analysis of statistical numbers of molecules or molecular assemblies supplies... 

Ginkgo s inhibitory effect on the production of amyloid-beta protein has also been mediated by other mechanisms, such as acetylcholinesterase inhibition, modulation of amyloid protein oligomeric species, and lowering of free cholesterol levels." ... 

VPl, previously shown to interact with some gangliosides, has recently been solved. In these experiments, recombinant VPl proteins oligomerized into pentameric structures that resemble capsid assemblies (Fig. 12.11). 

Griffith BR, Allen BL, Rapraeger AC, Kiessling LL (2004) A polymer scaffold for protein oligomerization. J Am Chem Soc 126 1608-1609... 

Urbane, B., Betnel, M., Cruz, L., Bitan, G., 8c Teplow, D. B. (2010). Elucidation of amyloid beta-protein oligomerization mechanisms Discrete molecular dynamics study. Journal of the American Chemical Society, 132, 4266. 

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