These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Journal Abstract Search


595 related items for PubMed ID: 11563917

  • 1. 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]

  • 2. Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates.
    Sato S, Kuhlman B, Wu WJ, Raleigh DP.
    Biochemistry; 1999 Apr 27; 38(17):5643-50. PubMed ID: 10220353
    [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. 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]

  • 5. NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9.
    Evans SP, Bycroft M.
    J Mol Biol; 1999 Aug 20; 291(3):661-9. PubMed ID: 10448044
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 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. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding.
    Kuhlman B, Boice JA, Fairman R, Raleigh DP.
    Biochemistry; 1998 Jan 27; 37(4):1025-32. PubMed ID: 9454593
    [Abstract] [Full Text] [Related]

  • 9. Domain behavior during the folding of a thermostable phosphoglycerate kinase.
    Parker MJ, Spencer J, Jackson GS, Burston SG, Hosszu LL, Craven CJ, Waltho JP, Clarke AR.
    Biochemistry; 1996 Dec 10; 35(49):15740-52. PubMed ID: 8961937
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. Kinetically robust monomeric protein from a hyperthermophile.
    Mukaiyama A, Takano K, Haruki M, Morikawa M, Kanaya S.
    Biochemistry; 2004 Nov 02; 43(43):13859-66. PubMed ID: 15504048
    [Abstract] [Full Text] [Related]

  • 12. An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability.
    Kuhlman B, Yang HY, Boice JA, Fairman R, Raleigh DP.
    J Mol Biol; 1997 Aug 01; 270(5):640-7. PubMed ID: 9245593
    [Abstract] [Full Text] [Related]

  • 13. 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 01; 7(9):1994-7. PubMed ID: 9761480
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. Crystal structure and structure-based mutational analyses of RNase HIII from Bacillus stearothermophilus: a new type 2 RNase H with TBP-like substrate-binding domain at the N terminus.
    Chon H, Matsumura H, Koga Y, Takano K, Kanaya S.
    J Mol Biol; 2006 Feb 10; 356(1):165-78. PubMed ID: 16343535
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H.
    Hollien J, Marqusee S.
    J Mol Biol; 2002 Feb 15; 316(2):327-40. PubMed ID: 11851342
    [Abstract] [Full Text] [Related]

  • 18. Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli.
    Chaudhuri TK, Horii K, Yoda T, Arai M, Nagata S, Terada TP, Uchiyama H, Ikura T, Tsumoto K, Kataoka H, Matsushima M, Kuwajima K, Kumagai I.
    J Mol Biol; 1999 Jan 22; 285(3):1179-94. PubMed ID: 9887272
    [Abstract] [Full Text] [Related]

  • 19. On the global architecture of initiation factor IF3: a comparative study of the linker regions from the Escherichia coli protein and the Bacillus stearothermophilus protein.
    Hua Y, Raleigh DP.
    J Mol Biol; 1998 May 15; 278(4):871-8. PubMed ID: 9614948
    [Abstract] [Full Text] [Related]

  • 20. 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]


    Page: [Next] [New Search]
    of 30.