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The Low-pH Unfolded State of the C-Terminal Domain of the Ribosomal Protein L9 Contains Significant Secondary Structure in the Absence of Denaturant but Is No More Compact Than the Low-pH Urea Unfolded State
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Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 36 checked references that resolve
resolves10.1016/j.jmb.2004.02.073
Thermodynamics and Kinetics of Non-native Interactions in Protein Folding: A Single Point Mutant Significantly Stabilizes the N-terminal Domain of L9 by Modulating Non-native Interactions in the Denatured State
resolves10.1006/jmbi.2001.4521
Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states11Edited by C. R. Matthews
resolves10.1016/j.jmb.2005.08.019
Mutational Analysis Demonstrates that Specific Electrostatic Interactions can Play a Key Role in the Denatured State Ensemble of Proteins
resolves10.1110/ps.9.7.1395
Charge–charge interactions influence the denatured state ensemble and contribute to protein stability
resolves10.1021/bi002776i
NMR Structural and Dynamic Characterization of the Acid-Unfolded State of Apomyoglobin Provides Insights into the Early Events in Protein Folding<sup>,</sup>
resolves10.1016/S0959-440X(96)80091-1
Structural analysis of non-native states of proteins by NMR methods
resolves10.1006/jmbi.2001.4750
Calculation of ensembles of structures representing the unfolded state of an SH3 domain
resolves10.1021/ja039250g
Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein
resolves10.1021/bi9627626
NMR Studies of Unfolded States of an SH3 Domain in Aqueous Solution and Denaturing Conditions
resolves10.1073/pnas.0403643101
Random-coil behavior and the dimensions of chemically unfolded proteins
resolves10.1016/S0065-3233(02)62012-1
Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
resolves10.1016/S0022-2836(03)00033-0
Computational Simulation of the Statistical Properties of Unfolded Proteins
resolves10.1038/nsb995
Structural correspondence between the α-helix and the random-flight chain resolves how unfolded proteins can have native-like properties
resolves10.1126/science.1523410
NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
resolves10.1021/bi061516j
Mutational Analysis of the Folding Transition State of the C-Terminal Domain of Ribosomal Protein L9: A Protein with an Unusual β-Sheet Topology
resolves10.1016/j.jmb.2005.04.017
Direct Characterization of the Folded, Unfolded and Urea-denatured States of the C-terminal Domain of the Ribosomal Protein L9
resolves10.1006/jmbi.1996.0696
Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR Spectroscopy
resolves10.1023/A:1008386816521
Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
resolves10.1007/BF00227471
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
resolves10.1110/ps.062465306
Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation
resolves10.1021/bi970049q
Structural and Dynamical Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M Urea
resolves10.1006/jmbi.1998.2145
Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters 1 1Edited by A. R. Fersht
resolves10.1021/bi9707133
Mechanism of Helix Induction by Trifluoroethanol: A Framework for Extrapolating the Helix-Forming Properties of Peptides from Trifluoroethanol/Water Mixtures Back to Water
resolves10.1006/jmbi.1999.2742
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed α/β protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9 1 1Edited by P. E. Wright
resolves10.1021/bi00185a040
Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation
resolves10.1007/BF00197809
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
The 4 references without a DOI — listed, not checked
no DOI — not checkedref22/cit22
no DOI — not checkedProtein NMR spectroscopy: Principles and practice
no DOI — not checkedref24/cit24
no DOI — not checkedref40/cit40
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