Heterogeneity in protein folding and unfolding reactions
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 …
Rules of physical mathematics govern intrinsically disordered proteins
In stark contrast to foldable proteins with a unique folded state, intrinsically disordered
proteins and regions (IDPs) persist in perpetually disordered ensembles. Yet an IDP …
proteins and regions (IDPs) persist in perpetually disordered ensembles. Yet an IDP …
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 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 …
Modern kinetics and mechanism of protein folding: A retrospective
WA Eaton - The Journal of Physical Chemistry B, 2021 - ACS Publications
Modern experimental kinetics of protein folding began in the early 1990s with the
introduction of nanosecond laser pulses to trigger the folding reaction, providing an almost …
introduction of nanosecond laser pulses to trigger the folding reaction, providing an almost …
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 …
Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions
I Peran, AS Holehouse, IS Carrico… - Proceedings of the …, 2019 - National Acad Sciences
Proteins are marginally stable molecules that fluctuate between folded and unfolded states.
Here, we provide a high-resolution description of unfolded states under refolding conditions …
Here, we provide a high-resolution description of unfolded states under refolding conditions …
A look back at the molten globule state of proteins: Thermodynamic aspects
Interest in protein folding intermediates lies in their significance to protein folding pathways.
The molten globule (MG) state is one such intermediate lying on the kinetic (and sometimes …
The molten globule (MG) state is one such intermediate lying on the kinetic (and sometimes …
Aggregates of fluorescent gels assembled by interfacial dynamic bonds
Z Hu, S Xu, H Zhang, X Ji - Aggregate, 2023 - Wiley Online Library
Life, defined as the specific form of substance, is an integration of aggregates at various
scales, ranging from single molecules to tissues. However, these building blocks of common …
scales, ranging from single molecules to tissues. However, these building blocks of common …
Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions
Macromolecular crowding effects on globular proteins, which usually adopt a single stable
fold, have been widely studied. However, little is known about crowding effects on fold …
fold, have been widely studied. However, little is known about crowding effects on fold …