| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2016PNAS..113E5389A |
| P356 | DOI | 10.1073/PNAS.1607193113 |
| P932 | PMC publication ID | 5027429 |
| P698 | PubMed publication ID | 27566405 |
| P50 | author | Andrea Soranno | Q42316865 |
| Benjamin Schuler | Q42316868 | ||
| Mikayel Aznauryan | Q42320745 | ||
| Jie-rong Huang | Q44885914 | ||
| Stephan Grzesiek | Q44958017 | ||
| P2093 | author name string | Daniel Nettels | |
| Alexander M Labhardt | |||
| Leonildo Delgado | |||
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| From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins. | Q34093140 | ||
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| Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations | Q35616340 | ||
| Ultrafast dynamics of protein collapse from single-molecule photon statistics. | Q35669661 | ||
| Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases | Q36279917 | ||
| Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy | Q36342960 | ||
| The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations | Q36379177 | ||
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| Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy | Q36445621 | ||
| Peptide chain dynamics in light and heavy water: zooming in on internal friction | Q45327991 | ||
| Quantitative modelfree analysis of urea binding to unfolded ubiquitin using a combination of small angle X-ray and neutron scattering. | Q45978446 | ||
| Single-molecule fluorescence studies of intrinsically disordered proteins. | Q46033026 | ||
| Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins | Q46440887 | ||
| Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH. | Q46791997 | ||
| Interaction of urea with amino acids: implications for urea-induced protein denaturation | Q46875424 | ||
| Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations | Q47630147 | ||
| Early collapse is not an obligate step in protein folding | Q47812546 | ||
| Effect of urea on the β-hairpin conformational ensemble and protein denaturation mechanism. | Q53088094 | ||
| Fifty years of solvent denaturation | Q53433405 | ||
| Rouse Model with Internal Friction: A Coarse Grained Framework for Single Biopolymer Dynamics | Q56829784 | ||
| Conformational distributions of unfolded polypeptides from novel NMR techniques | Q57080193 | ||
| Mapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar Couplings | Q57080200 | ||
| Direct Observation of Dipolar Couplings and Hydrogen Bonds across a β-Hairpin in 8 M Urea | Q57080206 | ||
| Long-Range Correlated Dynamics in Intrinsically Disordered Proteins | Q57712515 | ||
| Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells | Q57831648 | ||
| Motional properties of unfolded ubiquitin: a model for a random coil protein | Q58062241 | ||
| Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins | Q59332370 | ||
| Unfolded Protein and Peptide Dynamics Investigated with Single-Molecule FRET and Correlation Spectroscopy from Picoseconds to Seconds† | Q59332561 | ||
| Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels | Q73335302 | ||
| Effect of denaturing agents of the urea-guanidinium class on the solubility of acetyltetraglycine ethyl ester and related compounds | Q79606668 | ||
| NMR characterization of the dynamics of biomacromolecules | Q80435130 | ||
| Concerted dihedral rotations give rise to internal friction in unfolded proteins | Q87912069 | ||
| Small-Angle X-ray Scattering and Single-Molecule FRET Spectroscopy Produce Highly Divergent Views of the Low-Denaturant Unfolded State | Q36470871 | ||
| Atomic-level characterization of disordered protein ensembles | Q36717589 | ||
| Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin. | Q36772070 | ||
| Backbone Dynamics and Structural Characterization of the Partially Folded A State of Ubiquitin by 1H, 13C, and 15N Nuclear Magnetic Resonance Spectroscopy | Q36886625 | ||
| Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding | Q36964255 | ||
| Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form | Q37007122 | ||
| Collapse transition in proteins | Q37137234 | ||
| Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. | Q37153744 | ||
| Protein dynamics from single-molecule fluorescence intensity correlation functions | Q37397645 | ||
| Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins | Q37469603 | ||
| Reassessing random-coil statistics in unfolded proteins | Q37487200 | ||
| Random-coil behavior and the dimensions of chemically unfolded proteins | Q37493905 | ||
| Temperature-dependent solvation modulates the dimensions of disordered proteins | Q37702019 | ||
| Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering | Q37938727 | ||
| How, when and why proteins collapse: the relation to folding | Q37959224 | ||
| Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy | Q38203952 | ||
| Introducing protein intrinsic disorder | Q38205058 | ||
| Progress in studying intrinsically disordered proteins with atomistic simulations. | Q38392991 | ||
| Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods | Q39432831 | ||
| Exploring the role of internal friction in the dynamics of unfolded proteins using simple polymer models | Q39460391 | ||
| Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment. | Q41110746 | ||
| Pulsed interleaved excitation | Q42251940 | ||
| Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings | Q43162003 | ||
| Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings. | Q43243601 | ||
| Persistence of native-like topology in a denatured protein in 8 M urea | Q43682045 | ||
| Long-range interactions within a nonnative protein | Q43901723 | ||
| Demonstration by NMR of folding domains in lysozyme | Q44308247 | ||
| Multiple probes reveal a native-like intermediate during low-temperature refolding of ubiquitin | Q44926880 | ||
| P433 | issue | 37 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | E5389-98 | |
| P577 | publication date | 2016-08-26 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. | |
| P478 | volume | 113 |
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| Q49424214 | Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail |
| Q89741263 | Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy |
| Q41359094 | Combining NMR and small angle X-ray scattering for the study of biomolecular structure and dynamics. |
| Q47621056 | Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein. |
| Q93137829 | Commonly used FRET fluorophores promote collapse of an otherwise disordered protein |
| Q57180326 | Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE) |
| Q41293169 | Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements |
| Q34546157 | DisProt 7.0: a major update of the database of disordered proteins. |
| Q47236838 | Folding of maltose binding protein outside of and in GroEL. |
| Q90459885 | Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1 |
| Q87910173 | Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation |
| Q49990719 | Hypothesis: structural heterogeneity of the unfolded proteins originating from the coupling of the local clusters and the long-range distance distribution. |
| Q52329881 | Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function |
| Q59332309 | Inferring properties of disordered chains from FRET transfer efficiencies |
| Q57751774 | Local and non-local topological information in the denatured state ensemble of a β-barrel protein |
| Q89542344 | Molecular dynamics-derived rotamer libraries for d-amino acids within homochiral and heterochiral polypeptides |
| Q47106499 | Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths. |
| Q64869800 | Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein |
| Q89952853 | Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy |
| Q47778340 | SAXS versus FRET: A Matter of Heterogeneity? |
| Q52616567 | Simulation of FRET dyes allows quantitative comparison against experimental data. |
| Q58575706 | Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins |
| Q50577647 | Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A. |
| Q55164334 | Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. |
| Q96687783 | The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA |
| Q107112189 | The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA |
| Q92397223 | The combined force field-sampling problem in simulations of disordered amyloid-β peptides |
| Q39371374 | To be disordered or not to be disordered: is that still a question for proteins in the cell? |
| Q92547425 | Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions |
| Q47213644 | Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein. |
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