[HTML][HTML] Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversity

AA Bhopatkar, R Kayed - Journal of Biological Chemistry, 2023 - Elsevier
The β-sheet–rich amyloid core is the defining feature of protein aggregates associated with
neurodegenerative disorders. Recent investigations have revealed that there exist multiple …

[HTML][HTML] Applications of fluorescence spectroscopy in protein conformational changes and intermolecular contacts

FH dos Santos Rodrigues, GG Delgado, TS da Costa… - BBA advances, 2023 - Elsevier
Emission fluorescence is one of the most versatile and powerful biophysical techniques
used in several scientific subjects. It is extensively applied in the studies of proteins, their …

Towards design of drugs and delivery systems with the Martini coarse-grained model

LR Kjølbye, GP Pereira, A Bartocci, M Pannuzzo… - QRB …, 2022 - cambridge.org
Coarse-grained (CG) modelling with the Martini force field has come of age. By combining a
variety of bead types and sizes with a new map** approach, the newest version of the …

FRAP and FRET investigation of α-synuclein fibrillization via liquid-liquid phase separation in vitro and in HeLa cells

S Ray, N Singh, K Patel, G Krishnamoorthy… - … : Methods and Protocols, 2022 - Springer
Liquid-liquid phase separation (LLPS) acts as an important biological phenomenon in
membraneless organelle formation. These phase-separated bodies can also act as …

Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich Dimer

S Pal, JB Udgaonkar - Journal of Molecular Biology, 2024 - Elsevier
Misfolding of the prion protein is linked to multiple neurodegenerative diseases. A better
understanding of the process requires the identification and structural characterization of …

Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple ways

S Pal, JB Udgaonkar - Journal of Neurochemistry, 2023 - Wiley Online Library
The misfolding of the mammalian prion protein from its α‐helix rich cellular isoform to its β‐
sheet rich infectious isoform is associated with several neurodegenerative diseases. The …

Evolutionarily conserved proline residues impede the misfolding of the mouse prion protein by destabilizing an aggregation-competent partially unfolded form

S Pal, JB Udgaonkar - Journal of Molecular Biology, 2022 - Elsevier
The misfolding of the prion protein has been linked to several neurodegenerative diseases.
Despite extensive studies, the mechanism of the misfolding process remains poorly …

Rigidifying the β2− α2 Loop in the Mouse Prion Protein Slows down Formation of Misfolded Oligomers

S Pal, JB Udgaonkar - Biochemistry, 2024 - ACS Publications
Transmissible Spongiform Encephalopathies are fatal neurodegenerative diseases caused
by the misfolding of the cellular prion protein (PrPC) into its pathological isoform (PrPSc) …

Paramagnetic species in catalysis research: a unified approach towards (the role of EPR in) heterogeneous, homogeneous and enzyme catalysis

M Bracci, PC Bruzzese, A Famulari, D Fioco, A Guidetti… - 2020 - books.rsc.org
Paramagnetic (open-shell) systems, including transition metal ions, radical intermediates
and defect centres, are often involved in catalytic transformations. Despite the prevalence of …

Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases

L Mirdha, H Chakraborty - European Biophysics Journal, 2021 - Springer
Intrinsically disordered proteins (IDPs) have captured attention in the last couple of decades
due to their functional roles despite a lack of specific structure. Moreover, these proteins are …