Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy
The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …
with the realization that an unexpectedly high fraction of the human genome codes for …
Force field development and simulations of intrinsically disordered proteins
J Huang, AD MacKerell Jr - Current opinion in structural biology, 2018 - Elsevier
Highlights•General improvement of protein FFs leads to more accurate representation of
IDPs.•Increasing protein–water interaction allows sampling of more extended states of …
IDPs.•Increasing protein–water interaction allows sampling of more extended states of …
ALS mutations disrupt phase separation mediated by α-helical structure in the TDP-43 low-complexity C-terminal domain
RNA-binding protein TDP-43 mediates essential RNA processing but forms cytoplasmic
neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral sclerosis (ALS). It …
neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral sclerosis (ALS). It …
TDP-43 α-helical structure tunes liquid–liquid phase separation and function
Liquid–liquid phase separation (LLPS) is involved in the formation of membraneless
organelles (MLOs) associated with RNA processing. The RNA-binding protein TDP-43 is …
organelles (MLOs) associated with RNA processing. The RNA-binding protein TDP-43 is …
Balanced protein–water interactions improve properties of disordered proteins and non-specific protein association
Some frequently encountered deficiencies in all-atom molecular simulations, such as
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …
Temperature-dependent solvation modulates the dimensions of disordered proteins
For disordered proteins, the dimensions of the chain are an important property that is
sensitive to environmental conditions. We have used single-molecule Förster resonance …
sensitive to environmental conditions. We have used single-molecule Förster resonance …
Thermodynamically driven assemblies and liquid–liquid phase separations in biology
H Falahati, A Haji-Akbari - Soft matter, 2019 - pubs.rsc.org
The sustenance of life depends on the high degree of organization that prevails through
different levels of living organisms, from subcellular structures such as biomolecular …
different levels of living organisms, from subcellular structures such as biomolecular …
Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells
W Borcherds, FX Theillet, A Katzer, A Finzel… - Nature chemical …, 2014 - nature.com
Levels of residual structure in disordered interaction domains determine in vitro binding
affinities, but whether they exert similar roles in cells is not known. Here, we show that …
affinities, but whether they exert similar roles in cells is not known. Here, we show that …
Efficient atomistic simulation of pathways and calculation of rate constants for a protein–peptide binding process: Application to the MDM2 protein and an intrinsically …
MC Zwier, AJ Pratt, JL Adelman, JW Kaus… - The journal of …, 2016 - ACS Publications
The characterization of protein binding processes with all of the key conformational
changes has been a grand challenge in the field of biophysics. Here, we have used the …
changes has been a grand challenge in the field of biophysics. Here, we have used the …
Identification of dynamic modes in an intrinsically disordered protein using temperature-dependent NMR relaxation
The dynamic modes and time scales sampled by intrinsically disordered proteins (IDPs)
define their function. Nuclear magnetic resonance (NMR) spin relaxation is probably the …
define their function. Nuclear magnetic resonance (NMR) spin relaxation is probably the …