Relating sequence encoded information to form and function of intrinsically disordered proteins
Highlights•Compositions of IDPs fall into distinct classes.•Compositional classes encode
preferences for distinct conformational classes.•Functions of disordered proteins are …
preferences for distinct conformational classes.•Functions of disordered proteins are …
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 …
Distant residues modulate conformational opening in SARS-CoV-2 spike protein
D Ray, L Le, I Andricioaei - Proceedings of the National …, 2021 - National Acad Sciences
Infection by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) involves the
attachment of the receptor-binding domain (RBD) of its spike proteins to the ACE2 receptors …
attachment of the receptor-binding domain (RBD) of its spike proteins to the ACE2 receptors …
Structural origin of slow diffusion in protein folding
Experimental, theoretical, and computational studies of small proteins suggest that
interresidue contacts not present in the folded structure play little or no role in the self …
interresidue contacts not present in the folded structure play little or no role in the self …
Dynamics of proteins in solution
The dynamics of proteins in solution includes a variety of processes, such as backbone and
side-chain fluctuations, interdomain motions, as well as global rotational and translational …
side-chain fluctuations, interdomain motions, as well as global rotational and translational …
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 …
Fast protein folding is governed by memory-dependent friction
When described by a low-dimensional reaction coordinate, the folding rates of most proteins
are determined by a subtle interplay between free-energy barriers, which separate folded …
are determined by a subtle interplay between free-energy barriers, which separate folded …
Anisotropic friction in a ligand-protein complex
The effect of an externally applied directional force on molecular friction is so far poorly
understood. Here, we study the force-driven dissociation of the ligand-protein complex biotin …
understood. Here, we study the force-driven dissociation of the ligand-protein complex biotin …
Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations
The dynamics of proteins, which are essential for both folding and function, are known to be
strongly dependent on solvent viscosity or friction. However, an increasing number of …
strongly dependent on solvent viscosity or friction. However, an increasing number of …
A unified description of intrinsically disordered protein dynamics under physiological conditions using NMR spectroscopy
Intrinsically disordered proteins (IDPs) are flexible biomolecules whose essential functions
are defined by their dynamic nature. Nuclear magnetic resonance (NMR) spectroscopy is …
are defined by their dynamic nature. Nuclear magnetic resonance (NMR) spectroscopy is …