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

Mapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar Couplings is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/JA0724339
P698PubMed publication ID17636913

P50authorMartin BlackledgeQ21994149
Sebastian MeierQ43410284
Stephan GrzesiekQ44958017
P433issue31
P407language of work or nameEnglishQ1860
P304page(s)9799-9807
P577publication date2007-08-01
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleMapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar Couplings
P478volume129

Reverse relations

cites work (P2860)
Q517459483D J-resolved NMR spectroscopy for unstructured polypeptides: fast measurement of 3J HNH alpha coupling constants with outstanding spectral resolution.
Q37418779A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.
Q38589805Application of SAXS for the Structural Characterization of IDPs
Q35379375Application of the maximum entropy principle to determine ensembles of intrinsically disordered proteins from residual dipolar couplings
Q37264142Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Q57180326Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)
Q57080193Conformational distributions of unfolded polypeptides from novel NMR techniques
Q37924115Conformational propensities and residual structures in unfolded peptides and proteins
Q38116495Conformational propensities of intrinsically disordered proteins from NMR chemical shifts
Q44391914Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins
Q43658168Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating asx and β-type like turn conformations
Q35938545Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling
Q30353311Ensemble-based interpretations of NMR structural data to describe protein internal dynamics.
Q36132363Folding of Intrinsically Disordered Protein Phosphatase 1 Regulatory Proteins
Q38002804Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery
Q26851842Local order in the unfolded state: conformational biases and nearest neighbor interactions
Q30704962Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure.
Q33489161Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance
Q30372268Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.
Q38044416Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling
Q47316588Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering
Q37938727Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering
Q102369536Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy
Q38044412Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.
Q36558058Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.
Q55164334Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Q30407518The use of residual dipolar coupling in studying proteins by NMR.
Q37923322Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.
Q34005607What can solid state NMR contribute to our understanding of protein folding?
Q33635227beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin

Search more.