review article | Q7318358 |
scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0065-3233(02)62003-0 |
P698 | PubMed publication ID | 12418099 |
P2093 | author name string | David Shortle | |
P2860 | cites work | NMR structures of biomolecules using field oriented media and residual dipolar couplings | Q28203069 |
Conformation of Polypeptides and Proteins | Q29617878 | ||
Analysis of long-range interactions in a model denatured state of staphylococcal nuclease based on correlated changes in backbone dynamics | Q30175738 | ||
Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study | Q30194520 | ||
Principles of protein folding--a perspective from simple exact models. | Q30417429 | ||
Protein Denaturation | Q34221155 | ||
Nmr probes of molecular dynamics: overview and comparison with other techniques | Q34243213 | ||
Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states | Q34313193 | ||
Understanding how proteins fold: the lysozyme story so far. | Q34338183 | ||
A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease | Q36280149 | ||
Denatured states of proteins | Q37285327 | ||
Chemical shifts as a tool for structure determination | Q40576242 | ||
Structural analysis of non-native states of proteins by NMR methods | Q41026035 | ||
Composites of local structure propensities: evidence for local encoding of long-range structure | Q41790483 | ||
Persistence of native-like topology in a denatured protein in 8 M urea | Q43682045 | ||
Molecular alignment of denatured states of staphylococcal nuclease with strained polyacrylamide gels and surfactant liquid crystalline phases | Q43894603 | ||
A new approach for applying residual dipolar couplings as restraints in structure elucidation. | Q52578928 | ||
Dimensions of protein random coils | Q53019512 | ||
Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Delta131Delta, using NMR methods with improved resolution. | Q53698490 | ||
Are there pathways for protein folding? | Q64116226 | ||
Spin labeling of proteins | Q69362293 | ||
The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy | Q70782799 | ||
Why do protein architectures have Boltzmann-like statistics? | Q70980700 | ||
Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease | Q72732411 | ||
Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels | Q73335302 | ||
Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures | Q73335305 | ||
P304 | page(s) | 1-23 | |
P577 | publication date | 2002-01-01 | |
P1433 | published in | Advances in Protein Chemistry | Q15756442 |
P1476 | title | The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space | |
P478 | volume | 62 |
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Q33226011 | Building native protein conformation from highly approximate backbone torsion angles |
Q43256880 | Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein |
Q41825816 | Coarse-grained strategy for modeling protein stability in concentrated solutions. |
Q37854116 | Conformational dynamics of the molecular chaperone Hsp90 |
Q83275101 | Conformational isomers of denatured and unfolded proteins: methods of production and applications |
Q37924115 | Conformational propensities and residual structures in unfolded peptides and proteins |
Q34188142 | Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa |
Q30370558 | Denatured-state energy landscapes of a protein structural database reveal the energetic determinants of a framework model for folding. |
Q43658168 | Disorder 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 |
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Q49990719 | Hypothesis: structural heterogeneity of the unfolded proteins originating from the coupling of the local clusters and the long-range distance distribution. |
Q26851842 | Local order in the unfolded state: conformational biases and nearest neighbor interactions |
Q34913657 | Meeting halfway on the bridge between protein folding theory and experiment |
Q41941949 | Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions |
Q40093000 | Non-sequence-specific interactions can account for the compaction of proteins unfolded under "native" conditions. |
Q30342632 | Protein structure, stability and solubility in water and other solvents. |
Q79158487 | Structural correspondence between the alpha-helix and the random-flight chain resolves how unfolded proteins can have native-like properties |
Q35018042 | Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone |
Q51042630 | The HSP90 chaperone machinery. |
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Q30385084 | Understanding protein non-folding. |
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