Structural characterization of proteins and complexes using small-angle X-ray solution scattering

Mertens, Haydyn D. T.; Svergun, Dmitri I.

doi:10.1016/j.jsb.2010.06.012

Cited by 486 publications

(458 citation statements)

References 128 publications

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“…The Kratky plot of the SAXS scattering data (Fig. 3d) shows that, above the T t , combinations of ELP5 (0.008 mM) and PAK2 (0.174 mM) yielded a prominent peak typical of globular 'folded' proteins, but both ELP5/PAK3 and ELP5/PAK4 solutions showed a Kratky plot typical of partially 'unfolded' proteins 29 .…”

Section: Resultsmentioning

confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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ature uses self-assembly to create a widespread variety of complex structures with elaborate geometries and outstanding properties 1 such as hierarchical order, adaptability, selfhealing and bioactivity. Developing new bioinspired processes based on dynamic self-assembly could facilitate the fabrication of synthetic three-dimensional (3D) materials with enhanced complexity, dynamic properties and functionality 2 . Proteins are particularly attractive building blocks because of their versatility and biofunctionality 3 . Elastin-like polypeptides (ELPs) 4 are recombinant proteins that have generated great interest 5 as a result of their modular structure, bioactivity, ease of design and production, and the possibility to create robust and elastic materials 5,6 . ELPs allow for a tunable molecular design 7 and are based on the tropoelastin recurrent motif Val-Pro-Gly-X-Gly (VPGXG), in which X is any amino acid other than proline 7 . This repeating pentapeptide provides ELPs with a thermoresponsive behaviour. Below a critical transition temperature (T t ), the ELP molecule undergoes a reversible-phase transition wherein the protein is soluble in aqueous solution and becomes highly solvated, surrounded by clatharate-like water structures. Above the T t , the hydrophobic domains dehydrate and the protein chain hydrophobically collapses and aggregates to form a phaseseparated state 8 .The use of natural and synthetic proteins to create functional materials has been hindered by the difficulty in controlling their conformation and nanoscale assembly with the precision required to form macroscopic materials. This limitation has driven the development of simpler and more-predictable peptide-based materials 9,10 . Peptide amphiphiles (PAs), for example, are synthetic molecules that can self-assemble into nanofibres and create functional 3D hydrogels that emulate the fibrous architecture of the extracellular matrix (ECM) 11,12 . Nonetheless, most peptide and/or protein materials are formed through equilibrium-based self-assembly approaches that are capable of generating stable supramolecular structures, but with limited hierarchy and spatiotemporal control, which has hindered their functionality 2 .Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 . However, the possibility to exploit the unique structural and functional properties of proteins to create dynamic hierarchical materials remains an elusive target. In this study, we attempt to overcome this hurdle by using self-assembling peptides to promote protein conformational changes and guide their assembly into complex, yet functional, materials. We report the discovery and development of a protein/peptide system t...

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Section: Resultsmentioning

confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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“…The χ 2 (chi-square) test is widely used for scattering experiments because the basic assumption of this test, Gaussian distribution of uncertainties around a certain value, is fulfilled in SAS data. In this test the sum of squares of the differences between experimental and theoretical intensities is divided by the variance on each point, as shown below [7,17,30]:…”

Section: Modeling Methods For Sas Datamentioning

confidence: 99%

“…Further implementations performed for the use of ab initio methods applied to the study of macromolecules in solution took advantage of the known atomic resolution information for proteins, available in the protein data bank (https://www.wwpdb.org/) [47], and composes the ATSAS program suite [17,41,[57][58][59][60][61][62][63][64][65][66][67][68][69]. Several good reviews can be found in the literature for this subject [14,17,36,50,60,65,[67][68][69].…”

Section: Small Angle Scattering and Diffractionmentioning

confidence: 99%

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Calculation of Small-Angle Scattering Patterns

Alves¹,

Oliveira²

2018

Small Angle Scattering and Diffraction

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Small-angle scattering (SAS) experiments applied to nano-scaled systems allow the investigation of the constituents' overall shape, size, internal structure and arrangement. A standard scattering experiment requires a relatively simple setup and is often applied to investigate a system of particles. In these cases, the measured scattering intensity represents an average over a large number of particles illuminated by the incoming beam. The calculation and modeling of the scattering intensity can be performed by the use of analytical/semi-analytical expressions or by the use of numerical methods. In this book chapter, an overview of current available simulation/modeling methods for SAS will be shown either for systems composed of oriented or for randomly oriented particles. Examples demonstrating the use of the finite element method are presented as well as a newly developed method for calculating scattering intensity for oriented particles.

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“…The zero-angle scattering intensity, I(0) and the radius of gyration, R g , were calculated from data at very low q values (qR g Յ ϳ1.3) using the Guinier approximation (25)…”

Section: Methodsmentioning

confidence: 99%

Oligomerization, Membrane Association, and in Vivo Phosphorylation of Sugarcane UDP-glucose Pyrophosphorylase

Soares

Gentile

Scorsato

et al. 2014

Journal of Biological Chemistry

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Background: UDP-glucose pyrophosphorylase (UGPase) is a key enzyme in the biosynthesis of sucrose and the cell wall. Results: UGPase was phosphorylated in and associated with the membrane in vivo. Redox modification modulated UGPase activity by changing its oligomeric state. Conclusion: Phosphorylation, redox modification, and oligomerization regulate UGPase. Significance: Our data broaden the understanding of biomass biosynthesis in the bioenergy crop sugarcane.

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Structural characterization of proteins and complexes using small-angle X-ray solution scattering

Cited by 486 publications

References 128 publications

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Calculation of Small-Angle Scattering Patterns

Oligomerization, Membrane Association, and in Vivo Phosphorylation of Sugarcane UDP-glucose Pyrophosphorylase

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