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192 related items for PubMed ID: 23480024

  • 1. The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9.
    Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP.
    Biochemistry; 2013 Apr 16; 52(15):2662-71. PubMed ID: 23480024
    [Abstract] [Full Text] [Related]

  • 2. Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.
    Meng W, Raleigh DP.
    Proteins; 2011 Dec 16; 79(12):3500-10. PubMed ID: 21915914
    [Abstract] [Full Text] [Related]

  • 3. The unfolded state of NTL9 is compact in the absence of denaturant.
    Anil B, Li Y, Cho JH, Raleigh DP.
    Biochemistry; 2006 Aug 22; 45(33):10110-6. PubMed ID: 16906769
    [Abstract] [Full Text] [Related]

  • 4. Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9.
    Li Y, Picart F, Raleigh DP.
    J Mol Biol; 2005 Jun 17; 349(4):839-46. PubMed ID: 15890362
    [Abstract] [Full Text] [Related]

  • 5. Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure.
    Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV.
    Proc Natl Acad Sci U S A; 2013 Feb 05; 110(6):2123-8. PubMed ID: 23341588
    [Abstract] [Full Text] [Related]

  • 6. Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts.
    Luan B, Lyle N, Pappu RV, Raleigh DP.
    Biochemistry; 2014 Jan 14; 53(1):39-47. PubMed ID: 24280003
    [Abstract] [Full Text] [Related]

  • 7. The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure.
    Shan B, McClendon S, Rospigliosi C, Eliezer D, Raleigh DP.
    J Am Chem Soc; 2010 Apr 07; 132(13):4669-77. PubMed ID: 20225821
    [Abstract] [Full Text] [Related]

  • 8. Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins.
    Cho JH, Raleigh DP.
    J Mol Biol; 2005 Oct 14; 353(1):174-85. PubMed ID: 16165156
    [Abstract] [Full Text] [Related]

  • 9. 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.
    Cho JH, Sato S, Raleigh DP.
    J Mol Biol; 2004 May 07; 338(4):827-37. PubMed ID: 15099748
    [Abstract] [Full Text] [Related]

  • 10. 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.
    Li Y, Shan B, Raleigh DP.
    J Mol Biol; 2007 Apr 20; 368(1):256-62. PubMed ID: 17337003
    [Abstract] [Full Text] [Related]

  • 11. 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.
    Luisi DL, Wu WJ, Raleigh DP.
    J Mol Biol; 1999 Mar 26; 287(2):395-407. PubMed ID: 10080901
    [Abstract] [Full Text] [Related]

  • 12. Similarities between the spectrin SH3 domain denatured state and its folding transition state.
    Kortemme T, Kelly MJ, Kay LE, Forman-Kay J, Serrano L.
    J Mol Biol; 2000 Apr 14; 297(5):1217-29. PubMed ID: 10764585
    [Abstract] [Full Text] [Related]

  • 13. 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.
    Cho JH, Raleigh DP.
    J Mol Biol; 2006 Jun 23; 359(5):1437-46. PubMed ID: 16787780
    [Abstract] [Full Text] [Related]

  • 14. Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology.
    Li Y, Gupta R, Cho JH, Raleigh DP.
    Biochemistry; 2007 Jan 30; 46(4):1013-21. PubMed ID: 17240985
    [Abstract] [Full Text] [Related]

  • 15. Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding.
    Horng JC, Cho JH, Raleigh DP.
    J Mol Biol; 2005 Jan 07; 345(1):163-73. PubMed ID: 15567419
    [Abstract] [Full Text] [Related]

  • 16. pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding.
    Luisi DL, Raleigh DP.
    J Mol Biol; 2000 Jun 16; 299(4):1091-100. PubMed ID: 10843860
    [Abstract] [Full Text] [Related]

  • 17. On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9.
    Sato S, Xiang S, Raleigh DP.
    J Mol Biol; 2001 Sep 21; 312(3):569-77. PubMed ID: 11563917
    [Abstract] [Full Text] [Related]

  • 18. Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9.
    Luan B, Shan B, Baiz C, Tokmakoff A, Raleigh DP.
    Biochemistry; 2013 Apr 09; 52(14):2402-9. PubMed ID: 23461364
    [Abstract] [Full Text] [Related]

  • 19. The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models.
    Stenzoski NE, Zou J, Piserchio A, Ghose R, Holehouse AS, Raleigh DP.
    Biochemistry; 2020 Sep 15; 59(36):3290-3299. PubMed ID: 32786415
    [Abstract] [Full Text] [Related]

  • 20. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.
    Kuhlman B, Luisi DL, Young P, Raleigh DP.
    Biochemistry; 1999 Apr 13; 38(15):4896-903. PubMed ID: 10200179
    [Abstract] [Full Text] [Related]

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