[HTML][HTML] Computational methods to predict protein aggregation

S Navarro, S Ventura - Current Opinion in Structural Biology, 2022 - Elsevier
In most cases, protein aggregation stems from the establishment of non-native
intermolecular contacts. The formation of insoluble protein aggregates is associated with …

Functional amyloids from bacterial biofilms–structural properties and interaction partners

Ü Akbey, M Andreasen - Chemical Science, 2022 - pubs.rsc.org
Protein aggregation and amyloid formation have historically been linked with various
diseases such as Alzheimer's and Parkinson's disease, but recently functional amyloids …

Functional amyloids: Where supramolecular amyloid assembly controls biological activity or generates new functionality

JA Buchanan, NR Varghese, CL Johnston… - Journal of Molecular …, 2023 - Elsevier
Functional amyloids are a rapidly expanding class of fibrillar protein structures, with a core
cross-β scaffold, where novel and advantageous biological function is generated by the …

Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function

A Cembran, P Fernandez-Funez - Frontiers in Molecular …, 2023 - frontiersin.org
Prion diseases are fatal brain disorders characterized by deposition of insoluble isoforms of
the prion protein (PrP). The normal and pathogenic structures of PrP are relatively well …

The amyloid state of proteins: A boon or bane?

MN Hassan, F Nabi, AN Khan, M Hussain… - International Journal of …, 2022 - Elsevier
Proteins and their aggregation is significant field of research due to their association with
various conformational maladies including well-known neurodegenerative diseases like …

Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation

J Cámara-Almirón, L Domínguez-García… - npj Biofilms and …, 2023 - nature.com
Biofilms are bacterial communities that result from a cell differentiation process leading to
the secretion of an extracellular matrix (ECM) by part of the population. In Bacillus subtilis …

Analytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies

K Zumpfe, M Berbon, B Habenstein… - Journal of the …, 2024 - ACS Publications
Side-chain motions play an important role in understanding protein structure, dynamics,
protein–protein, and protein–ligand interactions. However, our understanding of protein side …

Atomic-Resolution Structure of the Protein Encoded by Gene V of Fd Bacteriophage in Complex with Viral ssDNA Determined by Magic-Angle Spinning Solid-State …

Y Shamir, A Goldbourt - Journal of the American Chemical Society, 2022 - ACS Publications
F-specific filamentous phages, elongated particles with circular single-stranded DNA
encased in a symmetric protein capsid, undergo an intermediate step, where thousands of …

Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis

E Lewkowicz, O Gursky - Biophysical chemistry, 2022 - Elsevier
Dynamic and disordered regions in native proteins are often critical for their function,
particularly in ligand binding and signaling. In certain proteins, however, such regions can …

The protein disorder cycle

VN Uversky - Biophysical Reviews, 2021 - Springer
This mini-review represents a brief, disorder-centric consideration of the interplay between
order and disorder in proteins. The goal here is to show that inside the cell, folding, non …