Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.

scientific article published on October 2012

Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1042/BST20120149
P698PubMed publication ID22988847

P50authorPau BernadóQ77491672
Nathalie SibilleQ57595167
P2093author name stringPau Bernadó
P2860cites workDetermination of Secondary Structure Populations in Disordered States of Proteins Using Nuclear Magnetic Resonance Chemical ShiftsQ57831878
Human Cardiac Myosin Binding Protein C: Structural Flexibility within an Extended Modular ArchitectureQ57979770
Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar CouplingsQ58484319
Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 ConceptQ22061726
Intrinsically unstructured proteins and their functionsQ22061731
Constructing ensembles for intrinsically disordered proteinsQ24616986
Determination of Multicomponent Protein Structures in Solution Using Global Orientation and Shape RestraintsQ27657269
Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray ScatteringQ27664132
Structure of the Vesicular Stomatitis Virus N0-P ComplexQ27674614
Tail-Mediated Collapse of HMGB1 Is Dynamic and Occurs via Differential Binding of the Acidic Tail to the A and B DomainsQ29395467
Intrinsic disorder and protein functionQ29616415
Structural characterization of flexible proteins using small-angle X-ray scatteringQ29617289
X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solutionQ29619405
Ensemble modeling of protein disordered states: experimental restraint contributions and validationQ30010207
Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraintsQ30157234
Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structureQ30158042
Weak alignment offers new NMR opportunities to study protein structure and dynamics.Q30332340
Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.Q30360720
Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls.Q30385150
Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR dataQ31020529
Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomesQ33252616
Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Q33671554
Conformational space of flexible biological macromolecules from average dataQ33686317
Sequence-specific random coil chemical shifts of intrinsically disordered proteinsQ33762545
Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligaseQ34074606
Use of chemical shifts in macromolecular structure determinationQ34084326
Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurementsQ34089470
Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.Q34092011
Multidomain assembled states of Hck tyrosine kinase in solutionQ34115671
A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.Q34144652
Changes in biomolecular conformation seen by small angle X-ray scatteringQ34440498
SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitionsQ34545957
Fuzzy complexes: polymorphism and structural disorder in protein-protein interactionsQ34720702
Intrinsic disorder in measles virus nucleocapsids.Q35049208
Molecular dynamics simulations of DNA curvature and flexibility: helix phasing and premeltingQ35645329
Polymer models of protein stability, folding, and interactions.Q35673797
Unfolded proteins and protein folding studied by NMR.Q35860163
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.Q36558058
Determination of conformationally heterogeneous states of proteinsQ36713680
The molecular sociology of the cellQ37030523
A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.Q37418779
Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplingsQ37596029
Protein NMR using paramagnetic ionsQ37749856
Structural characterization of proteins and complexes using small-angle X-ray solution scattering.Q37766020
Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.Q37923322
Structural analysis of intrinsically disordered proteins by small-angle X-ray scatteringQ37938727
How random are intrinsically disordered proteins? A small angle scattering perspectiveQ37951586
Intrinsically disordered proteins: from sequence and conformational properties toward drug discoveryQ38002804
Explaining the structural plasticity of α-synucleinQ39485110
The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 traffickingQ39572445
Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR RelaxationQ40625926
Modeling intrinsically disordered proteins with bayesian statisticsQ42408893
Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scatteringQ43605576
NMR spin relaxation methods for characterization of disorder and folding in proteinsQ43623358
Long-range interactions within a nonnative proteinQ43901723
Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding proteinQ44793886
Structural characterization of unfolded states of apomyoglobin using residual dipolar couplingsQ44966155
Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoproteinQ45394782
The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoproteinQ45728875
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domainsQ45796922
Structural characterization of the natively unfolded N-terminal domain of human c-Src kinase: insights into the role of phosphorylation of the unique domain.Q45972692
NMR analysis of a Tau phosphorylation patternQ46989797
On the origin of residual dipolar couplings from denatured proteinsQ47331925
Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables.Q47734327
Structural interpretation of paramagnetic relaxation enhancement-derived distances for disordered protein statesQ47787068
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins.Q51441407
NMR characterization of long-range order in intrinsically disordered proteins.Q51695027
Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complexQ52162421
Disorder and sequence repeats in hub proteins and their implications for network evolution.Q52673882
Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation.Q53285737
Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.Q53323738
Structural biology: Proteins in dynamic equilibrium.Q55053696
Small-angle scattering studies of biological macromolecules in solutionQ56444542
Mapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar CouplingsQ57080200
P433issue5
P304page(s)955-962
P577publication date2012-10-01
P1433published inBiochemical Society TransactionsQ864226
P1476titleStructural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS
P478volume40

Reverse relations

cites work (P2860)
Q47972812An Efficient Method for Estimating the Hydrodynamic Radius of Disordered Protein Conformations
Q51115133Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region.
Q22061736Classification of intrinsically disordered regions and proteins
Q64948601Comparative Exploratory Analysis of Intrinsically Disordered Protein Dynamics Using Machine Learning and Network Analytic Methods.
Q26798064Computational approaches for inferring the functions of intrinsically disordered proteins
Q27686991Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography
Q28681355Developing advanced X-ray scattering methods combined with crystallography and computation
Q38291388Emerging applications of small angle solution scattering in structural biology
Q40633455HN-NCA heteronuclear TOCSY-NH experiment for (1)H(N) and (15)N sequential correlations in ((13)C, (15)N) labelled intrinsically disordered proteins.
Q41098679High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations
Q24295282Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry
Q52329881Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function.
Q35510300Intrinsically disordered proteins in cellular signalling and regulation.
Q38044411Intrinsically disordered proteins: administration not executive.
Q54290264NMR structure analysis of uniformly 13C-labeled carbohydrates.
Q99234043ODiNPred: comprehensive prediction of protein order and disorder
Q31039692Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell
Q38810874Protein dynamics and function from solution state NMR spectroscopy
Q90233615Ratiometric Single-Molecule FRET Measurements to Probe Conformational Subpopulations of Intrinsically Disordered Proteins
Q39736764SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell
Q39846204SilE is an intrinsically disordered periplasmic "molecular sponge" involved in bacterial silver resistance
Q47316588Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering
Q38134535Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Q28074726Structural studies of RNA-protein complexes: A hybrid approach involving hydrodynamics, scattering, and computational methods
Q57814568The BackMAP Python module: how a simpler Ramachandran number can simplify the life of a protein simulator
Q28598253The Ramachandran Number: An Order Parameter for Protein Geometry
Q36283040The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil
Q47602277Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins
Q27301299Unveiling Inherent Degeneracies in Determining Population-Weighted Ensembles of Interdomain Orientational Distributions Using NMR Residual Dipolar Couplings: Application to RNA Helix Junction Helix Motifs
Q33701558Visualizing single-stranded nucleic acids in solution.
Q34406035p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.

Search more.