Using chemical shift perturbation to characterise ligand binding
MP Williamson - Progress in nuclear magnetic resonance spectroscopy, 2013 - Elsevier
Chemical shift perturbation (CSP, chemical shift map** or complexation-induced changes
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
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 …
Water dispersion interactions strongly influence simulated structural properties of disordered protein states
Many proteins can be partially or completely disordered under physiological conditions.
Structural characterization of these disordered states using experimental methods can be …
Structural characterization of these disordered states using experimental methods can be …
A soluble α-synuclein construct forms a dynamic tetramer
A heterologously expressed form of the human Parkinson disease-associated protein α-
synuclein with a 10-residue N-terminal extension is shown to form a stable tetramer in the …
synuclein with a 10-residue N-terminal extension is shown to form a stable tetramer in the …
Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
One of the major open challenges in structural biology is to achieve effective descriptions of
disordered states of proteins. This problem is difficult because these states are …
disordered states of proteins. This problem is difficult because these states are …
Sequence-specific random coil chemical shifts of intrinsically disordered proteins
Although intrinsically disordered proteins (IDPs) are widespread in nature and play diverse
and important roles in biology, they have to date been little characterized structurally …
and important roles in biology, they have to date been little characterized structurally …
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
M Kjaergaard, FM Poulsen - Journal of biomolecular NMR, 2011 - Springer
Random coil chemical shifts are necessary for secondary chemical shift analysis, which is
the main NMR method for identification of secondary structure in proteins. One of the largest …
the main NMR method for identification of secondary structure in proteins. One of the largest …
pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements
G Platzer, M Okon, LP McIntosh - Journal of biomolecular NMR, 2014 - Springer
The p K a values and charge states of ionizable residues in polypeptides and proteins are
frequently determined via NMR-monitored pH titrations. To aid the interpretation of the …
frequently determined via NMR-monitored pH titrations. To aid the interpretation of the …
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
M Kjaergaard, S Brander, FM Poulsen - Journal of biomolecular NMR, 2011 - Springer
Secondary chemical shift analysis is the main NMR method for detection of transiently
formed secondary structure in intrinsically disordered proteins. The quality of the secondary …
formed secondary structure in intrinsically disordered proteins. The quality of the secondary …
Injectable tissue integrating networks from recombinant polypeptides with tunable order
Emergent properties of natural biomaterials result from the collective effects of nanoscale
interactions among ordered and disordered domains. Here, using recombinant sequence …
interactions among ordered and disordered domains. Here, using recombinant sequence …