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127 related items for PubMed ID: 33576138
1. Investigating the folding mechanism of the N-terminal domain of ribosomal protein L9. Zhang H, Zhang H, Chen C. Proteins; 2021 Jul; 89(7):832-844. PubMed ID: 33576138 [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. 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]
4. 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]
5. 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]
6. 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]
7. 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]
8. 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]
9. 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]
10. Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9. Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP. J Mol Biol; 1999 May 28; 289(1):167-74. PubMed ID: 10339414 [Abstract] [Full Text] [Related]
11. 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. Vugmeyster L, Kuhlman B, Raleigh DP. Protein Sci; 1998 Sep 28; 7(9):1994-7. PubMed ID: 9761480 [Abstract] [Full Text] [Related]
12. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. Itzhaki LS, Otzen DE, Fersht AR. J Mol Biol; 1995 Nov 24; 254(2):260-88. PubMed ID: 7490748 [Abstract] [Full Text] [Related]
13. 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]
14. 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]
15. A molecular interpretation of 2D IR protein folding experiments with Markov state models. Baiz CR, Lin YS, Peng CS, Beauchamp KA, Voelz VA, Pande VS, Tokmakoff A. Biophys J; 2014 Mar 18; 106(6):1359-70. PubMed ID: 24655511 [Abstract] [Full Text] [Related]
16. pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain. Sato S, Luisi DL, Raleigh DP. Biochemistry; 2000 Apr 25; 39(16):4955-62. PubMed ID: 10769155 [Abstract] [Full Text] [Related]
17. High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States. Zhang Y, Kitazawa S, Peran I, Stenzoski N, McCallum SA, Raleigh DP, Royer CA. J Am Chem Soc; 2016 Nov 23; 138(46):15260-15266. PubMed ID: 27781428 [Abstract] [Full Text] [Related]
18. 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]
19. 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]
20. Folding dynamics of the Trp-cage miniprotein: evidence for a native-like intermediate from combined time-resolved vibrational spectroscopy and molecular dynamics simulations. Meuzelaar H, Marino KA, Huerta-Viga A, Panman MR, Smeenk LE, Kettelarij AJ, van Maarseveen JH, Timmerman P, Bolhuis PG, Woutersen S. J Phys Chem B; 2013 Oct 03; 117(39):11490-501. PubMed ID: 24050152 [Abstract] [Full Text] [Related] Page: [Next] [New Search]