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Collapse transitions of proteins and the interplay among backbone, sidechain, and solvent interactions
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 …
Conformational preferences and phase behavior of intrinsically disordered low complexity sequences: insights from multiscale simulations
Highlights•Low complexity (LC) sequences are prominent in eukaryotic proteomes.•LC
sequences are composed of a parsimonious subset of the naturally occurring amino …
sequences are composed of a parsimonious subset of the naturally occurring amino …
Sequence effects on size, shape, and structural heterogeneity in intrinsically disordered proteins
Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structures, thus
challenging the archetypal notion of structure–function relationships. Determining the …
challenging the archetypal notion of structure–function relationships. Determining the …
Collapse and Protein Folding: Should We Be Surprised that Biothermodynamics Works So Well?
A complete understanding of protein function and dynamics requires the characterization of
the multiple thermodynamic states, including the denatured state ensemble (DSE). Whereas …
the multiple thermodynamic states, including the denatured state ensemble (DSE). Whereas …
Commonly used FRET fluorophores promote collapse of an otherwise disordered protein
The dimensions that unfolded proteins, including intrinsically disordered proteins (IDPs),
adopt in the absence of denaturant remain controversial. We developed an analysis …
adopt in the absence of denaturant remain controversial. We developed an analysis …
The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins
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 …
Water as a good solvent for unfolded proteins: folding and collapse are fundamentally different
The argument that the hydrophobic effect is the primary effect driving the folding of globular
proteins is nearly universally accepted (including by the authors). But does this view also …
proteins is nearly universally accepted (including by the authors). But does this view also …
Hydrogen bonding patterns and cooperativity in polyproline II helical bundles
Hydrogen bond cooperativity (HBC) plays an important role in stabilizing protein assemblies
built by α-helices and β-sheets, the most common secondary structures. However, whether …
built by α-helices and β-sheets, the most common secondary structures. However, whether …
How hydrophobicity, side chains, and salt affect the dimensions of disordered proteins
Despite the generally accepted role of the hydrophobic effect as the driving force for folding,
many intrinsically disordered proteins (IDPs), including those with hydrophobic content …
many intrinsically disordered proteins (IDPs), including those with hydrophobic content …
The singular NMR fingerprint of a polyproline II helical bundle
Polyproline II (PPII) helices play vital roles in biochemical recognition events and structures
like collagen and form part of the conformational landscapes of intrinsically disordered …
like collagen and form part of the conformational landscapes of intrinsically disordered …