By Rubén Hervás, Albert Galera-Prat (auth.), Andres F. Oberhauser (eds.)
In Single Molecule experiences of Proteins, specialist researchers talk about the profitable program of single-molecule concepts to a variety of organic occasions, similar to the imaging and mapping of cellphone floor receptors, the research of the unfolding and folding pathways of unmarried proteins, the research interplay forces among biomolecules, the research of enzyme catalysis or the visualization of molecular vehicles in motion. The chapters are geared toward validated investigators and post-doctoral researchers within the lifestyles sciences eager to pursue learn within the a number of components within which single-molecule techniques are vital; this quantity additionally is still available to complex graduate scholars looking related learn goals.
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Extra resources for Single-molecule Studies of Proteins
Sample text
30 R. Herva´s et al. Fig. 4 Nanomechanics of IDPs by AFM–SMFS. (a) Nanomechanical analysis of pFS-2 +VAMP2. DLC (left) and F (right) histograms of pFS-2 polyproteins carrying VAMP2. This nonamyloidogenic IDP does not show conformational polymorphism. 6 mm. Figure taken with permission from Herva´s et al. 2012. (b) Schematic representation of the pFS-2 protein used in the carrier-guest strategy. The ubiquitin repeats are represented as gray boxes (U), followed by the number of the repeat in the construct.
Biophys J 92:22–233 Ainavarapu SRK, Wiita AP, Dougan L, Uggerud E, Fernandez JM (2008a) Single-molecule force spectroscopy measurements of bond elongation during a bimolecular reaction. J Am Chem Soc 130:6479–6487 Ainavarapu SRK, Wiita AP, Huang HH, Fernandez JM (2008b) A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding. J Am Chem Soc 130:436–437 Aioanei D, Lv S, Tessari I, Rampioni A, Bubacco L, Li H, Samorı` B, Brucale M (2011a) Singlemolecule-level evidence for the osmophobic effect.
2009). For the case of IDPs implicated in amyloid diseases (aka amyloidoses: disorders in which amyloid aggregates are formed), the conformational fluctuations in the monomer play an essential role in promoting the formation of early aggregates, which are critically associated to disease. The characterization of these conformational fluctuations in amyloidogenic proteins is fiendishly difficult for ensemble biophysical techniques. On the other hand, SMT are well suited for the task as they provide an unprecedented resolution that is extremely useful for investigating structural distributions and dynamics of complex biological systems.
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