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292 related items for PubMed ID: 15567419
1. 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]
2. 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]
3. 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]
4. 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]
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. 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]
7. 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]
8. 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]
9. 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]
10. 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]
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. Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. Grey MJ, Tang Y, Alexov E, McKnight CJ, Raleigh DP, Palmer AG. J Mol Biol; 2006 Feb 03; 355(5):1078-94. PubMed ID: 16332376 [Abstract] [Full Text] [Related]
13. 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]
14. 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]
15. Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. Barrick D, Hughson FM, Baldwin RL. J Mol Biol; 1994 Apr 15; 237(5):588-601. PubMed ID: 8158639 [Abstract] [Full Text] [Related]
16. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. Kuhlman B, Luisi DL, Evans PA, Raleigh DP. J Mol Biol; 1998 Dec 18; 284(5):1661-70. PubMed ID: 9878377 [Abstract] [Full Text] [Related]
17. 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]
18. pH dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure. Li Y, Horng JC, Raleigh DP. Biochemistry; 2006 Jul 18; 45(28):8499-506. PubMed ID: 16834323 [Abstract] [Full Text] [Related]
19. Kinetic analysis of molecular dynamics simulations reveals changes in the denatured state and switch of folding pathways upon single-point mutation of a beta-sheet miniprotein. Muff S, Caflisch A. Proteins; 2008 Mar 18; 70(4):1185-95. PubMed ID: 17847092 [Abstract] [Full Text] [Related]
20. Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization. Pierce MM, Nall BT. J Mol Biol; 2000 May 19; 298(5):955-69. PubMed ID: 10801361 [Abstract] [Full Text] [Related] Page: [Next] [New Search]