The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins
R Schweitzer-Stenner - Physical Chemistry Chemical Physics, 2023 - pubs.rsc.org
Over the last thirty years the unfolded state of proteins has attracted considerable interest
owing to the discovery of intrinsically disordered proteins which perform a plethora of …
owing to the discovery of intrinsically disordered proteins which perform a plethora of …
Realistic ensemble models of intrinsically disordered proteins using a structure-encoding coil database
Intrinsically disordered proteins (IDPs) play fundamental roles in signaling, regulation, and
cell homeostasis by specifically interacting with their partners. The structural characterization …
cell homeostasis by specifically interacting with their partners. The structural characterization …
Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding
Protein folding can be described as a motion of the polypeptide chain in a potential energy
funnel, where the conformational manifold is narrowed as the chain traverses from a …
funnel, where the conformational manifold is narrowed as the chain traverses from a …
Do molecular dynamics force fields accurately model Ramachandran distributions of amino acid residues in water?
Molecular dynamics (MD) is a powerful tool for studying intrinsically disordered proteins,
however, its reliability depends on the accuracy of the force field. We assess Amber ff19SB …
however, its reliability depends on the accuracy of the force field. We assess Amber ff19SB …
Short peptides as predictors for the structure of polyarginine sequences in disordered proteins
Intrinsically disordered proteins and intrinsically disordered regions are frequently enriched
in charged amino acids. Intrinsically disordered regions are regularly involved in important …
in charged amino acids. Intrinsically disordered regions are regularly involved in important …
Unravelling the effect of N (ε)-(carboxyethyl) lysine on the conformation, dynamics and aggregation propensity of α-synuclein
α-Synuclein (αS) aggregation is a hallmark in several neurodegenerative diseases. Among
them, Parkinson's disease is highlighted, characterized by the intraneuronal deposition of …
them, Parkinson's disease is highlighted, characterized by the intraneuronal deposition of …
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Using fine‐tuned hydrogen bonding criteria, a library of coiled peptide fragments has been
generated from a large set of high‐resolution protein X‐ray structures. This library is shown …
generated from a large set of high‐resolution protein X‐ray structures. This library is shown …
Dihedral angle preferences of amino acid residues forming various non-local interactions in proteins
In theory, a polypeptide chain can adopt a vast number of conformations, each
corresponding to a set of backbone rotation angles. Many of these conformations are …
corresponding to a set of backbone rotation angles. Many of these conformations are …
Anticooperative nearest-neighbor interactions between residues in unfolded peptides and proteins
Growing evidence suggests that the conformational distributions of amino acid residues in
unfolded peptides and proteins depend on the nature of the nearest neighbors. To explore …
unfolded peptides and proteins depend on the nature of the nearest neighbors. To explore …
Mutations in tau protein promote aggregation by favoring extended conformations
Amyloid aggregation of the intrinsically disordered protein (IDP) tau is involved in several
diseases, called tauopathies. Some tauopathies can be inherited due to mutations in the …
diseases, called tauopathies. Some tauopathies can be inherited due to mutations in the …