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

Wenli Meng; Bowu Luan; Nicholas Lyle; Rohit V. Pappu; Daniel P. Raleigh

doi:10.1021/bi301667u

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 ◽

10.1021/bi301667u ◽

2013 ◽

Vol 52 (15) ◽

pp. 2662-2671 ◽

Cited By ~ 22

Author(s):

Wenli Meng ◽

Bowu Luan ◽

Nicholas Lyle ◽

Rohit V. Pappu ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

Long Range ◽

Denatured State ◽

Terminal Domain ◽

Ribosomal Protein L9 ◽

State Ensemble

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Use of the Novel Fluorescent Amino Acidp-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 ◽

10.1021/bi7010674 ◽

2007 ◽

Vol 46 (43) ◽

pp. 12308-12313 ◽

Cited By ~ 41

Author(s):

Konstantinos N. Aprilakis ◽

Humeyra Taskent ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

The Novel ◽

Hydrophobic Core ◽

Core Formation ◽

Terminal Domain ◽

Ribosomal Protein L9

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

Biophysical Journal ◽

10.1016/j.bpj.2017.01.034 ◽

2017 ◽

Vol 112 (9) ◽

pp. 1797-1806 ◽

Cited By ~ 1

Author(s):

Satoshi Sato ◽

Jae-Hyun Cho ◽

Ivan Peran ◽

Rengin G. Soydaner-Azeloglu ◽

Daniel P. Raleigh

Keyword(s):

Transition State ◽

Ribosomal Protein ◽

Terminal Domain ◽

Ribosomal Protein L9

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

Biochemistry ◽

10.1021/bi972352x ◽

1998 ◽

Vol 37 (4) ◽

pp. 1025-1032 ◽

Cited By ~ 47

Author(s):

Brian Kuhlman ◽

Judith A. Boice ◽

Robert Fairman ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

Structure And Stability ◽

Terminal Domain ◽

Ribosomal Protein L9

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Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, ΔH°, ΔS°, and ΔC°p, and evaluation of solvent isotope effects

Protein Science ◽

10.1002/pro.5560071118 ◽

1998 ◽

Vol 7 (11) ◽

pp. 2405-2412 ◽

Cited By ~ 51

Author(s):

Brian Kuhlman ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

Thermodynamic Parameters ◽

Global Analysis ◽

Isotope Effects ◽

Chemical Denaturation ◽

Terminal Domain ◽

Ribosomal Protein L9 ◽

Solvent Isotope ◽

Solvent Isotope Effects

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Surface Salt Bridges, Double-Mutant Cycles, and Protein Stability: an Experimental and Computational Analysis of the Interaction of the Asp 23 Side Chain with the N-Terminus of the N-Terminal Domain of the Ribosomal Protein L9†

Biochemistry ◽

10.1021/bi027202n ◽

2003 ◽

Vol 42 (23) ◽

pp. 7050-7060 ◽

Cited By ~ 50

Author(s):

Donna L. Luisi ◽

Christopher D. Snow ◽

Jo-Jin Lin ◽

Zachary S. Hendsch ◽

Bruce Tidor ◽

...

Keyword(s):

Protein Stability ◽

Ribosomal Protein ◽

Double Mutant ◽

Computational Analysis ◽

Side Chain ◽

Salt Bridges ◽

Terminal Domain ◽

N Terminus ◽

Ribosomal Protein L9

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Investigating the folding mechanism of the N‐terminal domain of ribosomal protein L9

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.26062 ◽

2021 ◽

Author(s):

Haozhe Zhang ◽

Haomiao Zhang ◽

Changjun Chen

Keyword(s):

Ribosomal Protein ◽

Folding Mechanism ◽

Terminal Domain ◽

Ribosomal Protein L9

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pH Dependent Thermodynamic and Amide Exchange Studies of theC-Terminal Domain of the Ribosomal Protein L9: Implications for Unfolded State Structure†

Biochemistry ◽

10.1021/bi052534o ◽

2006 ◽

Vol 45 (28) ◽

pp. 8499-8506 ◽

Cited By ~ 6

Author(s):

Ying Li ◽

Jia-Cherng Horng ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

State Structure ◽

Terminal Domain ◽

Amide Exchange ◽

Unfolded State ◽

Ribosomal Protein L9 ◽

Ph Dependent

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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 ◽

10.1021/bi8006862 ◽

2008 ◽

Vol 47 (36) ◽

pp. 9565-9573 ◽

Cited By ~ 14

Author(s):

Bing Shan ◽

Shibani Bhattacharya ◽

David Eliezer ◽

Daniel P. Raleigh

Keyword(s):

Secondary Structure ◽

Ribosomal Protein ◽

Low Ph ◽

Terminal Domain ◽

Unfolded State ◽

Ribosomal Protein L9

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Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state 1 1Edited by P. E. Wright

Journal of Molecular Biology ◽

10.1006/jmbi.1999.2595 ◽

1999 ◽

Vol 287 (2) ◽

pp. 395-407 ◽

Cited By ~ 20

Author(s):

Donna L. Luisi ◽

Wen-Jin Wu ◽

Daniel P. Raleigh

Keyword(s):

Secondary Structure ◽

Conformational Analysis ◽

Ribosomal Protein ◽

Primary Sequence ◽

Terminal Domain ◽

Unfolded State ◽

Ribosomal Protein L9 ◽

State 1

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Amide proton exchange measurements as a probe of the stability and dynamics of the n-terminal domain of the ribosomal protein L9: Comparison with the intact protein

Protein Science ◽

10.1002/pro.5560070915 ◽

1998 ◽

Vol 7 (9) ◽

pp. 1994-1997 ◽

Cited By ~ 5

Author(s):

Liliya Vugmeyster ◽

Brian Kuhlman ◽

Daniel P. Raleigh

Keyword(s):

Ribosomal Protein ◽

Proton Exchange ◽

Amide Proton ◽

Intact Protein ◽

Terminal Domain ◽

Amide Proton Exchange ◽

Ribosomal Protein L9 ◽

The Stability

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