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 …
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …
G protein-coupled receptor kinases: Past, present and future
KE Komolov, JL Benovic - Cellular Signalling, 2018 - Elsevier
This review is provided in recognition of the extensive contributions of Dr. Robert J.
Lefkowitz to the G protein-coupled receptor (GPCR) field and to celebrate his 75th birthday …
Lefkowitz to the G protein-coupled receptor (GPCR) field and to celebrate his 75th birthday …
[PDF][PDF] 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update
In 2012, preliminary guidelines were published addressing sample quality, data acquisition
and reduction, presentation of scattering data and validation, and modelling for biomolecular …
and reduction, presentation of scattering data and validation, and modelling for biomolecular …
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 …
structure and structural transitions of biological macromolecules in solution. For folded …
Intrinsically disordered proteins: emerging interaction specialists
Highlights•Intrinsically disordered proteins mostly function by molecular recognition.•Post-
translational modifications regulate the interactions of IDPs.•Structural disorder can facilitate …
translational modifications regulate the interactions of IDPs.•Structural disorder can facilitate …
Multidomain assembled states of Hck tyrosine kinase in solution
S Yang, L Blachowicz, L Makowski… - Proceedings of the …, 2010 - National Acad Sciences
An approach combining small-angle X-ray solution scattering (SAXS) data with coarse-
grained (CG) simulations is developed to characterize the assembly states of Hck, a member …
grained (CG) simulations is developed to characterize the assembly states of Hck, a member …
Expanding the proteome: disordered and alternatively folded proteins
HJ Dyson - Quarterly reviews of biophysics, 2011 - cambridge.org
Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential
catalytic reactions. These characteristic functions have led us to presuppose that proteins …
catalytic reactions. These characteristic functions have led us to presuppose that proteins …
[HTML][HTML] SH2 domains: modulators of nonreceptor tyrosine kinase activity
The Src homology 2 (SH2) domain is a sequence-specific phosphotyrosine-binding module
present in many signaling molecules. In cytoplasmic tyrosine kinases, the SH2 domain is …
present in many signaling molecules. In cytoplasmic tyrosine kinases, the SH2 domain is …
Intramolecular fuzzy interactions involving intrinsically disordered domains
M Arbesú, G Iruela, H Fuentes, JMC Teixeira… - Frontiers in molecular …, 2018 - frontiersin.org
Structural disorder is an essential ingredient for function in many proteins and protein
complexes. Fuzzy complexes describe the many instances where disorder is maintained as …
complexes. Fuzzy complexes describe the many instances where disorder is maintained as …
Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering
P Bernadó - European Biophysics Journal, 2010 - Springer
Multidomain proteins in which consecutive globular regions are connected by linkers are
prevalent in nature (Levitt in Proc Natl Acad Sci USA 106: 11079–11084, 2009). Some …
prevalent in nature (Levitt in Proc Natl Acad Sci USA 106: 11079–11084, 2009). Some …