[HTML][HTML] A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins

AG Kikhney, DI Svergun - FEBS letters, 2015 - Elsevier
Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …

Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules …

GM Clore, J Iwahara - Chemical reviews, 2009 - ACS Publications
Understanding the function of biological macromolecules and their complexes at the
physicochemical level requires knowledge of both their structure and dynamics …

Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy

MR Jensen, M Zweckstetter, J Huang… - Chemical …, 2014 - ACS Publications
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 …

How random are intrinsically disordered proteins? A small angle scattering perspective

V Receveur-Bréchot, D Durand - Current Protein and Peptide …, 2012 - ingentaconnect.com
While the crucial role of intrinsically disordered proteins (IDPs) in the cell cycle is now
recognized, deciphering their molecular mode of action at the structural level still remains …

Visualizing transient dark states by NMR spectroscopy

NJ Anthis, GM Clore - Quarterly Reviews of Biophysics, 2015 - cambridge.org
Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering

P Bernado, DI Svergun - Molecular biosystems, 2012 - pubs.rsc.org
Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …

Dynamic protein interaction networks and new structural paradigms in signaling

V Csizmok, AV Follis, RW Kriwacki… - Chemical …, 2016 - ACS Publications
Understanding signaling and other complex biological processes requires elucidating the
critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent∼ …

Atomic-level characterization of disordered protein ensembles

T Mittag, JD Forman-Kay - Current opinion in structural biology, 2007 - Elsevier
The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …

NMR characterization of long-range order in intrinsically disordered proteins

L Salmon, G Nodet, V Ozenne, G Yin… - Journal of the …, 2010 - ACS Publications
Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of the
human genome, and the development of meaningful molecular descriptions of these …

Describing intrinsically disordered proteins at atomic resolution by NMR

MR Jensen, RWH Ruigrok, M Blackledge - Current opinion in structural …, 2013 - Elsevier
There is growing interest in the development of physical methods to study the
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …