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376 related items for PubMed ID: 16246369
1. 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]
2. 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]
3. 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]
4. Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d". Tripet B, Wagschal K, Lavigne P, Mant CT, Hodges RS. J Mol Biol; 2000 Jul 07; 300(2):377-402. PubMed ID: 10873472 [Abstract] [Full Text] [Related]
5. 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]
6. Hydrophobic core packing in the SH3 domain folding transition state. Northey JG, Di Nardo AA, Davidson AR. Nat Struct Biol; 2002 Feb 16; 9(2):126-30. PubMed ID: 11786916 [Abstract] [Full Text] [Related]
7. Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Colón W, Elöve GA, Wakem LP, Sherman F, Roder H. Biochemistry; 1996 Apr 30; 35(17):5538-49. PubMed ID: 8611545 [Abstract] [Full Text] [Related]
8. 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]
9. Differential stabilization of two hydrophobic cores in the transition state of the villin 14T folding reaction. Choe SE, Li L, Matsudaira PT, Wagner G, Shakhnovich EI. J Mol Biol; 2000 Nov 17; 304(1):99-115. PubMed ID: 11071813 [Abstract] [Full Text] [Related]
10. 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]
11. 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]
12. The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. Campbell-Valois FX, Michnick SW. J Mol Biol; 2007 Feb 02; 365(5):1559-77. PubMed ID: 17137592 [Abstract] [Full Text] [Related]
13. 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]
14. Context-dependent nature of destabilizing mutations on the stability of FKBP12. Main ER, Fulton KF, Jackson SE. Biochemistry; 1998 Apr 28; 37(17):6145-53. PubMed ID: 9558354 [Abstract] [Full Text] [Related]
15. 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]
16. 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]
17. Understanding the mechanism of beta-hairpin folding via phi-value analysis. Du D, Tucker MJ, Gai F. Biochemistry; 2006 Feb 28; 45(8):2668-78. PubMed ID: 16489760 [Abstract] [Full Text] [Related]
18. The nature of the free energy barriers to two-state folding. Akmal A, Muñoz V. Proteins; 2004 Oct 01; 57(1):142-52. PubMed ID: 15326600 [Abstract] [Full Text] [Related]
19. Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. Northey JG, Maxwell KL, Davidson AR. J Mol Biol; 2002 Jul 05; 320(2):389-402. PubMed ID: 12079394 [Abstract] [Full Text] [Related]
20. Functional impact of polar and acidic substitutions in the lactose repressor hydrophobic monomer.monomer interface with a buried lysine. Zhan H, Sun Z, Matthews KS. Biochemistry; 2009 Feb 17; 48(6):1305-14. PubMed ID: 19166325 [Abstract] [Full Text] [Related] Page: [Next] [New Search]