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 …
Describing sequence–ensemble relationships for intrinsically disordered proteins
Intrinsically disordered proteins participate in important protein–protein and protein–nucleic
acid interactions and control cellular phenotypes through their prominence as dynamic …
acid interactions and control cellular phenotypes through their prominence as dynamic …
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 …
NMR provides unique insight into the functional dynamics and interactions of intrinsically disordered proteins
AR Camacho-Zarco, V Schnapka, S Guseva… - Chemical …, 2022 - ACS Publications
Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing
essential roles in all aspects of cellular and extracellular biochemistry. To understand their …
essential roles in all aspects of cellular and extracellular biochemistry. To understand their …
Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments
Over the last two decades, it has become increasingly clear that a large fraction of the
human proteome is intrinsically disordered or contains disordered segments of significant …
human proteome is intrinsically disordered or contains disordered segments of significant …
Conformational propensities of intrinsically disordered proteins from NMR chemical shifts
The realization that a protein can be fully functional even in the absence of a stable three‐
dimensional structure has motivated a large number of studies describing the …
dimensional structure has motivated a large number of studies describing the …
A maximum entropy approach to the study of residue‐specific backbone angle distributions in α‐synuclein, an intrinsically disordered protein
Abstract α‐Synuclein is an intrinsically disordered protein of 140 residues that switches to an
α‐helical conformation upon binding phospholipid membranes. We characterize its residue …
α‐helical conformation upon binding phospholipid membranes. We characterize its residue …
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental
approaches for investigating the conformational behaviour of intrinsically disordered …
approaches for investigating the conformational behaviour of intrinsically disordered …
Local order in the unfolded state: conformational biases and nearest neighbor interactions
S Toal, R Schweitzer-Stenner - Biomolecules, 2014 - mdpi.com
The discovery of Intrinsically Disordered Proteins, which contain significant levels of disorder
yet perform complex biologically functions, as well as unwanted aggregation, has motivated …
yet perform complex biologically functions, as well as unwanted aggregation, has motivated …
Secondary structure assignment for conformationally irregular peptides: Comparison between DSSP, STRIDE and KAKSI
Secondary structure assignment codes were built to explore the regularities associated with
the periodic motifs of proteins, such as those in backbone dihedral angles or in hydrogen …
the periodic motifs of proteins, such as those in backbone dihedral angles or in hydrogen …