Highlights•Mutational effects are consistently felt beyond the first shell of
interactions.•Mutations modulate the dynamics and chemical shifts of distal …

Despite the recent advances in the prediction of protein structures by deep neutral networks,
the elucidation of protein-folding mechanisms remains challenging. A promising theory for …

A longstanding goal in the field of intrinsically disordered proteins (IDPs) is to characterize
their structural heterogeneity and pinpoint the role of this heterogeneity in IDP function …

TipA, a MerR family transcription factor from Streptomyces lividans, promotes antibiotic
resistance by sequestering broad-spectrum thiopeptide-based antibiotics, thus …

Statistical mechanical models that afford an intermediate resolution between macroscopic
chemical models and all-atom simulations have been successful in capturing folding …

Over 40% of eukaryotic proteomes and 15% of bacterial proteomes are predicted to be
intrinsically disordered based on their amino acid sequence. Intrinsically disordered proteins …

The relative magnitudes of noncovalent stabilization energies or the coupling free energies
in folded proteins are anisotropically distributed, uniquely influencing folding and functional …

We investigate the conformational properties of the intrinsically disordered DNA-binding
domain of CytR in the presence of the polymeric crowder polyethylene glycol (PEG) …

The intrinsically disordered DNA-binding domain of cytidine repressor (CytR-DBD) folds in
the presence of target DNA and regulates the expression of multiple genes in E. coli. To …

Structural disorder in proteins arises from a complex interplay between weak hydrophobicity
and unfavorable electrostatic interactions. The extent to which the hydrophobic effect …