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Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

Proceedings of the National Academy of Sciences - PNAS, 2013-02, Vol.110 (6), p.2123-2128

2013

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Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

Angewandte Chemie (International ed.), 2010-10, Vol.49 (41), p.7473-7475

2010

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Cooperative Cold Denaturation: The Case of the C‑Terminal Domain of Ribosomal Protein L9

Biochemistry (Easton), 2013-04, Vol.52 (14), p.2402-2409

2013

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The Denatured State Ensemble Contains Significant Local and Long-Range Structure under Native Conditions: Analysis of the N‑Terminal Domain of Ribosomal Protein L9

Biochemistry (Easton), 2013-04, Vol.52 (15), p.2662-2671

2013

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The Unfolded State of the C-Terminal Domain of the Ribosomal Protein L9 Contains Both Native and Non-Native Structure

Biochemistry (Easton), 2009-06, Vol.48 (22), p.4707-4719

2009

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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

Journal of molecular biology, 2004-05, Vol.338 (4), p.827-837

2004

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Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions

Proceedings of the National Academy of Sciences - PNAS, 2019-06, Vol.116 (25), p.12301-12310

2019

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The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9

Journal of molecular biology, 2007-04, Vol.368 (1), p.256-262

2007

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Electrostatic Interactions in the Denatured State and in the Transition State for Protein Folding: Effects of Denatured State Interactions on the Analysis of Transition State Structure

Journal of molecular biology, 2006-06, Vol.359 (5), p.1437-1446

2006

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The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models

Biochemistry (Easton), 2020-09, Vol.59 (36), p.3290-3299

2020

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High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States

Journal of the American Chemical Society, 2016-11, Vol.138 (46), p.15260-15266

2016

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The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures

Biophysical journal, 2018-08, Vol.115 (4), p.655-663

2018

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Direct Characterization of the Folded, Unfolded and Urea-denatured States of the C-terminal Domain of the Ribosomal Protein L9

Journal of molecular biology, 2005-06, Vol.349 (4), p.839-846

2005

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Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9

Biochemistry (Easton), 2016-04, Vol.55 (15), p.2251-2259

2016

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Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions

Proteins, structure, function, and bioinformatics, 2011-12, Vol.79 (12), p.3500-3510

2011

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Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates

Biophysical journal, 2019-02, Vol.116 (3), p.445-453

2019

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Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure

Biochemistry (Easton), 2017-02, Vol.56 (8), p.1085-1094

2017

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Denatured State Ensembles with the Same Radii of Gyration Can Form Significantly Different Long-Range Contacts

Biochemistry (Easton), 2014-01, Vol.53 (1), p.39-47

2014

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The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State

Biophysical journal, 2017-05, Vol.112 (9), p.1797-1806

2017

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The Cold Denatured State of the C-terminal Domain of Protein L9 Is Compact and Contains Both Native and Non-native Structure

Journal of the American Chemical Society, 2010-04, Vol.132 (13), p.4669-4677

2010

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Interpretation of p-Cyanophenylalanine Fluorescence in Proteins in Terms of Solvent Exposure and Contribution of Side-Chain Quenchers: A Combined Fluorescence, IR and Molecular Dynamics Study

Biochemistry (Easton), 2009-09, Vol.48 (38), p.9040-9046

2009

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Mutational Analysis Demonstrates that Specific Electrostatic Interactions can Play a Key Role in the Denatured State Ensemble of Proteins

Journal of molecular biology, 2005-10, Vol.353 (1), p.174-185

2005

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Use of the Novel Fluorescent Amino Acid p-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding

Biochemistry (Easton), 2007-10, Vol.46 (43), p.12308-12313

2007

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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

Biochemistry (Easton), 2008-09, Vol.47 (36), p.9565-9573

2008

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Structure and Stability of the N-Terminal Domain of the Ribosomal Protein L9: Evidence for Rapid Two-State Folding

Biochemistry (Easton), 1998-01, Vol.37 (4), p.1025-1032

1998

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Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

Cooperative Cold Denaturation: The Case of the C‑Terminal Domain of Ribosomal Protein L9

The Denatured State Ensemble Contains Significant Local and Long-Range Structure under Native Conditions: Analysis of the N‑Terminal Domain of Ribosomal Protein L9

The Unfolded State of the C-Terminal Domain of the Ribosomal Protein L9 Contains Both Native and Non-Native Structure

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

Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions

The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9

Electrostatic Interactions in the Denatured State and in the Transition State for Protein Folding: Effects of Denatured State Interactions on the Analysis of Transition State Structure

The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models

High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States

The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures

Direct Characterization of the Folded, Unfolded and Urea-denatured States of the C-terminal Domain of the Ribosomal Protein L9

Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9

Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions

Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates

Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure

Denatured State Ensembles with the Same Radii of Gyration Can Form Significantly Different Long-Range Contacts

The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State

The Cold Denatured State of the C-terminal Domain of Protein L9 Is Compact and Contains Both Native and Non-native Structure

Interpretation of p-Cyanophenylalanine Fluorescence in Proteins in Terms of Solvent Exposure and Contribution of Side-Chain Quenchers: A Combined Fluorescence, IR and Molecular Dynamics Study

Mutational Analysis Demonstrates that Specific Electrostatic Interactions can Play a Key Role in the Denatured State Ensemble of Proteins

Use of the Novel Fluorescent Amino Acid p-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding

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

Structure and Stability of the N-Terminal Domain of the Ribosomal Protein L9: Evidence for Rapid Two-State Folding

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