Amyloid fibrils are attractive targets for applications in biotechnology. These thin, nanoscale protein fibers are highly ordered structures that self-assemble from their component proteins or peptides. This chapter describes the use of several biophysical techniques to monitor the formation of amyloid fibrils including a common dye-binding assay, turbidity assay, and small-angle X-ray scattering. These techniques provide information about the assembly mechanism, the rate and reproducibility of assembly, as well as the size of species along the assembly pathway. © 2013 Springer Science+Business Media, New York
Many proteins of diverse sequence, structure and function self-assemble into morphologically similar...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...
This journal is © The Royal Society of Chemistry 2014Self-assembling amyloid-like peptides and prote...
Bioinspired and bioinorganic materials sciences offer unique opportunities to produce and manipulate...
Bioinspired and bioinorganic materials sciences offer unique opportunities to produce and manipulate...
The self-assembly of soluble proteins into amyloid aggregates is a mechanism which can be observed i...
Amyloid formation is a fascinating process with both biomedical and materials science relevance. Amy...
This journal is © The Royal Society of Chemistry 2014Self-assembling amyloid-like peptides and prote...
Protein and peptide self-assembly is integral to a growing number of misfolding diseases that involv...
© 2014 American Chemical Society. In this study, amyloid fibers prepared from hen egg white lysozyme...
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide ...
The ability of short peptide fragments to self-assemble in isolation as amyloid and amyloid-like str...
The use of self-assembling peptides as scaffolds for creating biomaterials has prompted the scientif...
Nature materials achieve structural complexity by inducing a network of molecules into forming elabo...
Many proteins of diverse sequence, structure and function self-assemble into morphologically similar...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...
This journal is © The Royal Society of Chemistry 2014Self-assembling amyloid-like peptides and prote...
Bioinspired and bioinorganic materials sciences offer unique opportunities to produce and manipulate...
Bioinspired and bioinorganic materials sciences offer unique opportunities to produce and manipulate...
The self-assembly of soluble proteins into amyloid aggregates is a mechanism which can be observed i...
Amyloid formation is a fascinating process with both biomedical and materials science relevance. Amy...
This journal is © The Royal Society of Chemistry 2014Self-assembling amyloid-like peptides and prote...
Protein and peptide self-assembly is integral to a growing number of misfolding diseases that involv...
© 2014 American Chemical Society. In this study, amyloid fibers prepared from hen egg white lysozyme...
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide ...
The ability of short peptide fragments to self-assemble in isolation as amyloid and amyloid-like str...
The use of self-assembling peptides as scaffolds for creating biomaterials has prompted the scientif...
Nature materials achieve structural complexity by inducing a network of molecules into forming elabo...
Many proteins of diverse sequence, structure and function self-assemble into morphologically similar...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human...