Results 81 to 90 of about 202,201 (346)

Analysis of XFEL serial diffraction data from individual crystalline fibrils [PDF]

open access: yes, 2017
Serial diffraction data collected at the Linac Coherent Light Source from crystalline amyloid fibrils delivered in a liquid jet show that the fibrils are well oriented in the jet.

core   +1 more source

Smaller is better: nanobodies meet NMR

open access: yesFEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

Prion Amyloid Polymorphs – The Tag Might Change It All

open access: yesFrontiers in Molecular Biosciences, 2020
Sup35p is a protein from Saccharomyces cerevisiae. It can propagate using a prion-like mechanism, which means that it can recruit non-prion soluble Sup35p into insoluble fibrils.
Luc Bousset   +7 more
doaj   +1 more source

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates [PDF]

open access: yes, 2023
Tau protein fibrillization is implicated in the pathogenesis of several neurodegenerative diseases collectively known as Tauopathies. For decades, investigating Tau fibrillization in vitro has required the addition of polyanions or other co-factors to ...
Meltem Tatli   +35 more
core   +1 more source

Eumelanin fibrils

open access: yesJournal of Biomedical Optics, 2012
We describe the auto-oxidation of 3, 4-dihydroxy-L-phenylalanine (L-DOPA) in the synthesis of eumelanin to spontaneously produce fibrils upon drying. The self-assembled fibrils are of characteristic diameter ∼1 to 2 μm, composed of filaments, and are unidirectional, apart from branches that are formed at typically an angle of 20 to 22 deg.
McQueenie, Ross   +3 more
openaire   +4 more sources

Invisible but not inaccessible—Revealing transient oligomers formed by intrinsically disordered proteins with solution NMR and complementary methods

open access: yesFEBS Letters, EarlyView.
Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley   +1 more source

Self-assembling nanomaterials: monitoring the formation of amyloid fibrils, with a focus on small-angle X-ray scattering.

open access: yes, 2013
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.
Gras, Sally L   +5 more
core   +2 more sources

Fibrils

open access: yes, 2016
In this study, structural and mechanical properties of a series of models of Aβ42 (one‐ and two‐fold) and Aβ40 (two‐ and three‐fold) fibrils have been computed by using all‐atom molecular dynamics simulations. Based on calculations of the twist angle (θ)
Zachary Hoffmann   +13 more
core   +1 more source

TEM images of self-assembled fibrils.

open access: yes, 2020
A-C) RiAFP-m9 fibrils formed after incubation at 37 °C. The arrow indicates the twist of a single fibril. D) SBAFP-CT fibrils. Scale bar: A) 500 nm; B) 200 nm (resolution 3.5–3.8 nm); C) 60 nm; D) 100 nm.
Maria D. R. Peralta (4568749)   +3 more
core   +1 more source

Going viral − Virus‐targeting nanobodies for research, diagnostics and therapy

open access: yesFEBS Letters, EarlyView.
The increasing prevalence of viral diseases represents a major threat for global human health. Nanobodies, small binding fragments derived from camelid heavy‐chain antibodies, offer versatile tools for viral research, diagnostics, and antiviral therapy.
Domenic Ebert, Ulrich Rothbauer
wiley   +1 more source

Home - About - Disclaimer - Privacy