| scholarly article | Q13442814 |
| P356 | DOI | 10.1039/C6MB00489J |
| P698 | PubMed publication ID | 27545097 |
| P50 | author | Reinhard Schweitzer-Stenner | Q39189033 |
| P2093 | author name string | Siobhan E Toal | |
| P2860 | cites work | Chemical shifts as a tool for structure determination | Q40576242 |
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| NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein | Q57889927 | ||
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| Structure and Dynamics of the Homologous Series of Alanine Peptides: A Joint Molecular Dynamics/NMR Study | Q58062171 | ||
| Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar Couplings | Q58484319 | ||
| The Alzheimer β-peptide shows temperature-dependent transitions between left-handed 31-helix, β-strand and random coil secondary structures | Q58486515 | ||
| Neighbor-dependent Ramachandran probability distributions of amino acids developed from a hierarchical Dirichlet process model | Q21145340 | ||
| A protein factor essential for microtubule assembly | Q22010837 | ||
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| Structural characterization of flexible proteins using small-angle X-ray scattering | Q29617289 | ||
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| Molecular Dynamics Simulations of 441 Two-Residue Peptides in Aqueous Solution: Conformational Preferences and Neighboring Residue Effects with the Amber ff99SB-ildn-NMR Force Field | Q31025559 | ||
| Origin of the neighboring residue effect on peptide backbone conformation | Q31094215 | ||
| Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library | Q33218650 | ||
| Statistical coil model of the unfolded state: resolving the reconciliation problem | Q33222591 | ||
| Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants | Q33412499 | ||
| Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants | Q33518834 | ||
| Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution. | Q33891175 | ||
| Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts. | Q34092011 | ||
| A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. | Q34144652 | ||
| Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales | Q34212739 | ||
| Protein Denaturation | Q34221155 | ||
| Ionized trilysine: a model system for understanding the nonrandom structure of poly-L-lysine and lysine-containing motifs in proteins | Q34308982 | ||
| Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains | Q34508241 | ||
| The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development | Q34577841 | ||
| pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study | Q34601824 | ||
| Conformation of the backbone in unfolded proteins. | Q36472811 | ||
| 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 | Q36671524 | ||
| 'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. | Q36718622 | ||
| Reassessing random-coil statistics in unfolded proteins | Q37487200 | ||
| Conformational propensities and residual structures in unfolded peptides and proteins | Q37924115 | ||
| Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy | Q38203952 | ||
| A simple model for polyproline II structure in unfolded states of alanine-based peptides | Q38270402 | ||
| P433 | issue | 11 | |
| P921 | main subject | statistics | Q12483 |
| nearest neighbour algorithm | Q1374523 | ||
| P1104 | number of pages | 13 | |
| P304 | page(s) | 3294-3306 | |
| P577 | publication date | 2016-08-22 | |
| P1433 | published in | Molecular BioSystems | Q3319467 |
| P1476 | title | Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides | |
| P478 | volume | 12 |
| Q88055727 | Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins |
| Q50961220 | Dihedral angle preferences of amino acid residues forming various non-local interactions in proteins. |
| Q47835787 | Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. |
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