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2368 Juárez et al. and hence causing the alignment of filaments to become less accurate. Such unspecific effects may contribute to morphological differences in any protein’s amyloid samples induced at high temperature. In this regard, recent reports based on nuclear magnetic resonance showed that different fibril morphologies have different underlying secondary structures, and as such are likely produced by distinct independent assembly pathways (93,94). A summary of the various fibril morphologies observed in this study is shown in Fig. 12 together with a schematic representation of the assembly process. We propose that at elevated temperature (except at pH 3.0 in the absence of electrolyte), HSA forms rapidly globular oligomers that upon mutual interaction evolve into more elongated structures (bead-like) that grow to protofibrils either by subsequent annealing of oligomers and/or protein monomers. Mature fibrils can be formed by lateral association of protofibrils or the addition of protein oligomers to the growing fibril, both at the ends of the fibril and by lateral fusion. Ringlike structures are present in acidic conditions at elevated temperature in the presence of electrolyte as an additional intermediate state formed by association of short bead-like structures, which disappears when protofibrils are observed in solution. Thus, we think that they may act as reservoirs of initially very short protofibrils. CONCLUSIONS We observed the formation of protofibrils, curly fibers, and mature fibrils by the protein HSA under different solution conditions. We analyzed the fibrillation process and the conformational changes associated with it by using different spectroscopic techniques, and confirmed the necessary development of b-sheet structure upon fibrillation. In addition, the shapes of the different structural intermediates and final products in the fibrillation process were observed by TEM, SEM, and AFM. The obtained fibrils show structural features typical of classical amyloid fibers, as denoted by XRD, CD, and fluorescence spectroscopies, and TEM. A model of fibril formation based on the elongation of protein oligomers through mutual interactions and subsequent annealing and growth is FIGURE 12 Mechanisms of fibril formation for HSA. Biophysical Journal 96(6) 2353–2370 presented. Nevertheless, some differences in the fibrillation mechanism occur depending on the solution conditions; for example, ring-shaped structures are observed only as a structural intermediate under acidic conditions in the presence of added electrolyte. SUPPORTING MATERIAL Ten figures and a table are available at http://www.biophysj.org/biophysj/ supplemental/S0006-3495(09)00322-1. We thank Dr. Eugenio Vázquez for his assistance with the CD measurements. This study was supported by the Ministerio de Educación y Ciencia (project MAT-2007-61604). REFERENCES 1. Reches, M., and E. Gazit. 2003. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science. 300:625–627. 2. Rajagopal, K., and J. P. Schneider. 2004. Self-assembling peptides and proteins for nanotechnological applications. Curr. Opin. Struct. Biol. 14:480–486. 3. Stefani, M., and C. M. Dobson. 2003. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81:678–699. 4. Soto, C., L. Estrada, and J. Castilla. 2006. Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem. Sci. 31:150–155. 5. Khurana, R., C. Ionescu-Zanetti, M. Pope, J. Li, L. Nelson, et al. 2003. A general mode for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophys. J. 85:1135–1144. 6. Chiti, F., M. Stefani, N. Taddei, G. 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Grupo de Física de Coloides y Pol
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Agradecimientos A mi Familia A mi P
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v List of papers I. Self-assembly p
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2.3 2.4 2.5 2.6 2.7 2.8 2.9 2.10 2.
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5.4 5.5 5.3.2 5.5.1 Chapter 6 Kinet
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amiloides de la proteína albúmina
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vesiculares son el resultado de la
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origina debido a condiciones ambien
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con las fibras vecinas más cercana
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Abstract In the present work, we in
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[Au]/[protein] molar ratio and numb
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synthetic polymers are obtained fro
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On the other hand, in terms of chem
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Additionally, to obtain a better kn
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therefore, characteristic of solid
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presence of electrostatic charge in
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Contents 2.1 2.2 2.3 2.4 2.5 2.6 2.
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where w is the meniscus’ weight d
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that they exert little force one on
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This oscillating dipole acts as an
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(APD) and its associated optics (pi
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where r is the distance of the dipo
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When , the former equation can be s
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autocorrelation function (ACF). In
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and, therefore, . The autocorrelati
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A transmission electron microscope
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2.5.- Atomic force microscopy (AFM)
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ecause of the energy loss in the ex
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Figure 2.15. Schematic representati
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ackbone of proteins. Since proteins
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According to classical mechanics, t
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chemical composition, configuration
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2.9.1.- Viscoelasticity Many materi
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where is the total strain rate, whi
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Using equations 2.40 and 2.41 in eq
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scattering process that incoming X-
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maximum intensity of the peak, Imax
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translation of the reciprocal latti
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For a single crystal, the chance to
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excitation; namely, a valance elect
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Figure 2.27. Distinction between si
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microscope, there are two polarized
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In particular, we use SQUID to meas
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are aligned by means of an external
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on the digital profile of a drop im
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Laser confocal microscopy. Confocal
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Fluorescence spectroscopy. Fluoresc
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Superconducting quantum interferenc
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temperatures, the chains are mixed
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e detected by a given method. Therm
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subsequently, of their thermodynami
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a) O b) H 2C CH 2 O H 2C CH Figure
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Contents 4.1 4.2 4.3 4.3.1 CHAPTER
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7108 Langmuir, Vol. 24, No. 14, 200
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One-Dimensional Magnetic Nanowires
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One-Dimensional Magnetic Nanowires
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temperatures, and solvent polarity.
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Conclusions The work has two parts:
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equire a highly organized and unsta
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References 1. Hiemenz, Paul C. Poly
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33. Wang, Z. L. HANDBOOK OF MICROSC
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67. Polymers Get Organized. Bucknal
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94. Are there Pathways for Protein
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123. Designing conditions for in vi
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151. SERS-based diagnosis and biode
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