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136 related items for PubMed ID: 8639683

  • 1. Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase.
    Saab-Rincón G, Gualfetti PJ, Matthews CR.
    Biochemistry; 1996 Feb 13; 35(6):1988-94. PubMed ID: 8639683
    [Abstract] [Full Text] [Related]

  • 2. Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.
    Ogasahara K, Yutani K.
    Biochemistry; 1997 Jan 28; 36(4):932-40. PubMed ID: 9020793
    [Abstract] [Full Text] [Related]

  • 3. Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration.
    Saab-Rincón G, Froebe CL, Matthews CR.
    Biochemistry; 1993 Dec 21; 32(50):13981-90. PubMed ID: 8268176
    [Abstract] [Full Text] [Related]

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  • 5. Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein.
    Shao X, Hensley P, Matthews CR.
    Biochemistry; 1997 Aug 12; 36(32):9941-9. PubMed ID: 9245428
    [Abstract] [Full Text] [Related]

  • 6. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
    Gualfetti PJ, Bilsel O, Matthews CR.
    Protein Sci; 1999 Aug 12; 8(8):1623-35. PubMed ID: 10452606
    [Abstract] [Full Text] [Related]

  • 7. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.
    Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR.
    Biochemistry; 1999 Jan 19; 38(3):1018-29. PubMed ID: 9893998
    [Abstract] [Full Text] [Related]

  • 8. Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase.
    Hurle MR, Michelotti GA, Crisanti MM, Matthews CR.
    Proteins; 1987 Jan 19; 2(1):54-63. PubMed ID: 3328859
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  • 9. Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry.
    Rojsajjakul T, Wintrode P, Vadrevu R, Robert Matthews C, Smith DL.
    J Mol Biol; 2004 Jul 30; 341(1):241-53. PubMed ID: 15312776
    [Abstract] [Full Text] [Related]

  • 10. Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study.
    Hoeltzli SD, Frieden C.
    Biochemistry; 1998 Jan 06; 37(1):387-98. PubMed ID: 9425060
    [Abstract] [Full Text] [Related]

  • 11. Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate.
    Shao X, Matthews CR.
    Biochemistry; 1998 May 26; 37(21):7850-8. PubMed ID: 9601046
    [Abstract] [Full Text] [Related]

  • 12. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein.
    Zitzewitz JA, Matthews CR.
    Biochemistry; 1999 Aug 03; 38(31):10205-14. PubMed ID: 10433729
    [Abstract] [Full Text] [Related]

  • 13. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein.
    Gualfetti PJ, Iwakura M, Lee JC, Kihara H, Bilsel O, Zitzewitz JA, Matthews CR.
    Biochemistry; 1999 Oct 05; 38(40):13367-78. PubMed ID: 10529212
    [Abstract] [Full Text] [Related]

  • 14. Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone.
    Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K.
    Biochemistry; 2005 Feb 01; 44(4):1184-92. PubMed ID: 15667212
    [Abstract] [Full Text] [Related]

  • 15. Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.
    Rhee S, Miles EW, Mozzarelli A, Davies DR.
    Biochemistry; 1998 Jul 28; 37(30):10653-9. PubMed ID: 9692955
    [Abstract] [Full Text] [Related]

  • 16. Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants.
    Ionescu RM, Eftink MR.
    Biochemistry; 1997 Feb 04; 36(5):1129-40. PubMed ID: 9033404
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  • 18. Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein.
    Wu Y, Vadrevu R, Yang X, Matthews CR.
    J Mol Biol; 2005 Aug 19; 351(3):445-52. PubMed ID: 16023136
    [Abstract] [Full Text] [Related]

  • 19. Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli.
    Jeong MS, Jeong JK, Lim WK, Jang SB.
    Biochem Biophys Res Commun; 2004 Oct 29; 323(4):1257-64. PubMed ID: 15451433
    [Abstract] [Full Text] [Related]

  • 20. Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX).
    Tafer H, Hiller S, Hilty C, Fernández C, Wüthrich K.
    Biochemistry; 2004 Feb 03; 43(4):860-9. PubMed ID: 14744128
    [Abstract] [Full Text] [Related]

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