Conformational propensities of intrinsically disordered proteins from NMR chemical shifts (Q38116495)

29 August 2017

title

Conformational propensities of intrinsically disordered proteins from NMR chemical shifts (English)

1 reference

Malene Ringkjøbing Jensen

29 August 2017

author

series ordinal

4

object named as

Malene Ringkjøbing Jensen

0 references

Martin Blackledge

series ordinal

3

object named as

Martin Blackledge

1 reference

29 August 2017

Jaka Kragelj

1

1 reference

29 August 2017

Valéry Ozenne

series ordinal

2

1 reference

29 August 2017

language of work or name

1 reference

21 June 2013

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29 August 2017

1 reference

29 August 2017

volume

14

1 reference

29 August 2017

issue

13

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29 August 2017

page(s)

3034-3045

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Natively unfolded proteins: a point where biology waits for physics

29 August 2017

cites work

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Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes

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Unusual biophysics of intrinsically disordered proteins

21 January 2018

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Recognition between flexible protein molecules: induced and assisted folding

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Coupling of folding and binding for unstructured proteins

21 January 2018

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Mechanism of coupled folding and binding of an intrinsically disordered protein

21 January 2018

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Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'.

21 January 2018

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Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners

21 January 2018

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Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions

21 January 2018

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Fuzziness: linking regulation to protein dynamics

21 January 2018

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Folding and binding cascades: dynamic landscapes and population shifts

21 January 2018

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Structured disorder and conformational selection

21 January 2018

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Preformed structural elements feature in partner recognition by intrinsically unstructured proteins

21 January 2018

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https://api.crossref.org/works/10.1002%2FCPHC.201300387

Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein

21 January 2018

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https://api.crossref.org/works/10.1002%2FCPHC.201300387

Describing sequence-ensemble relationships for intrinsically disordered proteins

21 January 2018

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https://api.crossref.org/works/10.1002%2FCPHC.201300387

Unfolded proteins and protein folding studied by NMR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Atomic-level characterization of disordered protein ensembles

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Biophysical characterization of intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.

21 January 2018

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https://api.crossref.org/works/10.1002%2FCPHC.201300387

Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Probing the diverse landscape of protein flexibility and binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Describing intrinsically disordered proteins at atomic resolution by NMR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Speeding up three-dimensional protein NMR experiments to a few minutes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Cooling overall spin temperature: protein NMR experiments optimized for longitudinal relaxation effects

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

A set of BEST triple-resonance experiments for time-optimized protein resonance assignment.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Automatic assignment of the intrinsically disordered protein Tau with 441-residues.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Sparsely sampled high-resolution 4-D experiments for efficient backbone resonance assignment of disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

4D non-uniformly sampled HCBCACON and ¹J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

HA-detected experiments for the backbone assignment of intrinsically disordered proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural characterization of the natively unfolded N-terminal domain of human c-Src kinase: insights into the role of phosphorylation of the unique domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Chemical shifts as a tool for structure determination

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Chemical shifts and three-dimensional protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Chemical shifts in biomolecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Disordered proteins studied by chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Automated prediction of 15N, 13Calpha, 13Cbeta and 13C' chemical shifts in proteins using a density functional database

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Automated 1H and 13C chemical shift prediction using the BioMagResBank

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

SHIFTX2: significantly improved protein chemical shift prediction

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

SPARTA+: a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Fast and accurate predictions of protein NMR chemical shifts from interatomic distances.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Enhanced conformational space sampling improves the prediction of chemical shifts in proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Interpreting protein structural dynamics from NMR chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Protein structure determination from NMR chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Consistent blind protein structure generation from NMR chemical shift data

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Sequence-dependent correction of random coil NMR chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Chemical shift prediction for denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Probability-based protein secondary structure identification using combined NMR chemical-shift data

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

RefDB: a database of uniformly referenced protein chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Sequence-specific random coil chemical shifts of intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Quantitative modelfree analysis of urea binding to unfolded ubiquitin using a combination of small angle X-ray and neutron scattering.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Conformation of the backbone in unfolded proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Circular dichroism spectrum of peptides in the poly(Pro)II conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Statistical coil model of the unfolded state: resolving the reconciliation problem

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Conformational distributions of unfolded polypeptides from novel NMR techniques

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Calculation of ensembles of structures representing the unfolded state of an SH3 domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Ensemble modeling of protein disordered states: experimental restraint contributions and validation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Characterization of disordered proteins with ENSEMBLE.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural signature of the MYPT1-PP1 interaction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Modeling intrinsically disordered proteins with bayesian statistics

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Constructing ensembles for intrinsically disordered proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Explaining the structural plasticity of α-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

A soluble α-synuclein construct forms a dynamic tetramer

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

The dynamic structure of α-synuclein multimers.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Mapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar Couplings

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural characterization of alpha-synuclein in an aggregation prone state.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

NMR characterization of long-range order in intrinsically disordered proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural impact of proline-directed pseudophosphorylation at AT8, AT100, and PHF1 epitopes on 441-residue tau.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Structural basis for the attachment of a paramyxoviral polymerase to its template

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Intrinsic disorder in measles virus nucleocapsids.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

On the origin of NMR dipolar waves in transient helical elements of partially folded proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Speeding up sequence specific assignment of IDPs

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Novel 13C direct detection experiments, including extension to the third dimension, to perform the complete assignment of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Protonless NMR Experiments for Sequence-Specific Assignment of Backbone Nuclei in Unfolded Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

13C-detected protonless NMR spectroscopy of proteins in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Accurate Random Coil Chemical Shifts from an Analysis of Loop Regions in Native States of Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

Determination of Secondary Structure Populations in Disordered States of Proteins Using Nuclear Magnetic Resonance Chemical Shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Alpha proton detection based backbone assignment of intrinsically disordered proteins

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Investigation of the neighboring residue effects on protein chemical shifts

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein

1 reference

https://api.crossref.org/works/10.1002%2FCPHC.201300387

7 January 2021

Identifiers

DOI

10.1002/CPHC.201300387

1 reference

29 August 2017

1 reference