Classification of intrinsically disordered regions and proteins

R Van Der Lee, M Buljan, B Lang, RJ Weatheritt… - Chemical …, 2014 - ACS Publications
Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

Unusual biophysics of intrinsically disordered proteins

VN Uversky - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2013 - Elsevier
Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …

[HTML][HTML] Phosphodiesterase 5 (PDE5): Structure-function regulation and therapeutic applications of inhibitors

WS Ahmed, AM Geethakumari, KH Biswas - Biomedicine & …, 2021 - Elsevier
Abstract Phosphodiesterase 5 (PDE5) is one of the most well-studied phosphodiesterases
(PDEs) that specifically targets cGMP typically generated by nitric oxide (NO)-mediated …

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 …

Linking folding and binding

PE Wright, HJ Dyson - Current opinion in structural biology, 2009 - Elsevier
Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part,
upon binding to their physiological targets. The past few years have seen an exponential …

Intrinsically disordered proteins from A to Z

VN Uversky - The international journal of biochemistry & cell biology, 2011 - Elsevier
The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …

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 …

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 …

[图书][B] Introduction to proteins: structure, function, and motion

A Kessel, N Ben-Tal - 2018 - taylorfrancis.com
Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

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∼ …