Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins
The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …
Cosolvent effects on protein stability
Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …
solution can easily be altered by the addition of small organic molecules known as …
Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water
A substantial fraction of the proteome is intrinsically disordered, and even well-folded
proteins adopt non-native geometries during synthesis, folding, transport, and turnover …
proteins adopt non-native geometries during synthesis, folding, transport, and turnover …
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements
Unfolded states of proteins and native states of intrinsically disordered proteins (IDPs)
populate heterogeneous conformational ensembles in solution. The average sizes of these …
populate heterogeneous conformational ensembles in solution. The average sizes of these …
Heterogeneity in protein folding and unfolding reactions
S Bhatia, JB Udgaonkar - Chemical Reviews, 2022 - ACS Publications
Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …
Consistent view of polypeptide chain expansion in chemical denaturants from multiple experimental methods
There has been a long-standing controversy regarding the effect of chemical denaturants on
the dimensions of unfolded and intrinsically disordered proteins: A wide range of …
the dimensions of unfolded and intrinsically disordered proteins: A wide range of …
Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS
M Aznauryan, L Delgado, A Soranno… - Proceedings of the …, 2016 - National Acad Sciences
The properties of unfolded proteins are essential both for the mechanisms of protein folding
and for the function of the large group of intrinsically disordered proteins. However, the …
and for the function of the large group of intrinsically disordered proteins. However, the …
Quantitative description of intrinsically disordered proteins using single-molecule FRET, NMR, and SAXS
S Naudi-Fabra, M Tengo, MR Jensen… - Journal of the …, 2021 - ACS Publications
Studying the conformational landscape of intrinsically disordered and partially folded
proteins is challenging and only accessible to a few solution state techniques, such as …
proteins is challenging and only accessible to a few solution state techniques, such as …
Collapse transitions of proteins and the interplay among backbone, sidechain, and solvent interactions
AS Holehouse, RV Pappu - Annual Review of biophysics, 2018 - annualreviews.org
Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like
conformations. Additionally, they can fold into well-defined three-dimensional structures or …
conformations. Additionally, they can fold into well-defined three-dimensional structures or …
Probing the action of chemical denaturant on an intrinsically disordered protein by simulation and experiment
Chemical denaturants are the most commonly used agents for unfolding proteins and are
thought to act by better solvating the unfolded state. Improved solvation is expected to lead …
thought to act by better solvating the unfolded state. Improved solvation is expected to lead …