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179 related items for PubMed ID: 28494951
1. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP. Biophys J; 2017 May 09; 112(9):1797-1806. PubMed ID: 28494951 [Abstract] [Full Text] [Related]
2. 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]
3. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9. Sato S, Raleigh DP. J Mol Biol; 2007 Jul 06; 370(2):349-55. PubMed ID: 17512540 [Abstract] [Full Text] [Related]
4. 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]
5. 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]
6. 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]
7. pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. Sato S, Raleigh DP. J Mol Biol; 2002 Apr 26; 318(2):571-82. PubMed ID: 12051860 [Abstract] [Full Text] [Related]
8. 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]
9. Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. Anil B, Sato S, Cho JH, Raleigh DP. J Mol Biol; 2005 Dec 02; 354(3):693-705. PubMed ID: 16246369 [Abstract] [Full Text] [Related]
10. 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]
11. 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. Aprilakis KN, Taskent H, Raleigh DP. Biochemistry; 2007 Oct 30; 46(43):12308-13. PubMed ID: 17924662 [Abstract] [Full Text] [Related]
12. Investigating the folding mechanism of the N-terminal domain of ribosomal protein L9. Zhang H, Zhang H, Chen C. Proteins; 2021 Jul 30; 89(7):832-844. PubMed ID: 33576138 [Abstract] [Full Text] [Related]
13. Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Horng JC, Moroz V, Rigotti DJ, Fairman R, Raleigh DP. Biochemistry; 2002 Nov 12; 41(45):13360-9. PubMed ID: 12416980 [Abstract] [Full Text] [Related]
14. 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]
15. Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state. Otzen DE, Oliveberg M. J Mol Biol; 2002 Apr 05; 317(4):613-27. PubMed ID: 11955013 [Abstract] [Full Text] [Related]
16. Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Taskent H, Cho JH, Raleigh DP. J Mol Biol; 2008 May 02; 378(3):699-706. PubMed ID: 18384809 [Abstract] [Full Text] [Related]
17. Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. Horng JC, Moroz V, Raleigh DP. J Mol Biol; 2003 Feb 28; 326(4):1261-70. PubMed ID: 12589767 [Abstract] [Full Text] [Related]
18. 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]
19. Nascent β-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts. Chen W, Shi C, Shen J. Biophys J; 2015 Aug 04; 109(3):630-8. PubMed ID: 26244744 [Abstract] [Full Text] [Related]
20. 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] Page: [Next] [New Search]