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Journal Abstract Search

243 related items for PubMed ID: 2872918

  • 1. Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli.
    Beasty AM, Hurle MR, Manz JT, Stackhouse T, Onuffer JJ, Matthews CR.
    Biochemistry; 1986 May 20; 25(10):2965-74. PubMed ID: 2872918
    [Abstract] [Full Text] [Related]

  • 2. Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase.
    Matthews CR, Crisanti MM, Manz JT, Gepner GL.
    Biochemistry; 1983 Mar 15; 22(6):1445-52. PubMed ID: 6132619
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  • 3. Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase.
    Tsuji T, Chrunyk BA, Chen X, Matthews CR.
    Biochemistry; 1993 Jun 01; 32(21):5566-75. PubMed ID: 8504078
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  • 4. Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase.
    Hurle MR, Tweedy NB, Matthews CR.
    Biochemistry; 1986 Oct 21; 25(21):6356-60. PubMed ID: 3539187
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  • 5. Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction.
    Tweedy NB, Hurle MR, Chrunyk BA, Matthews CR.
    Biochemistry; 1990 Feb 13; 29(6):1539-45. PubMed ID: 2185841
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  • 6. Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase.
    Choi SG, Hardman JK.
    J Biol Chem; 1995 Nov 24; 270(47):28177-82. PubMed ID: 7499309
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  • 7. Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.
    Stackhouse TM, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW.
    Biochemistry; 1988 Jan 26; 27(2):824-32. PubMed ID: 3280027
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  • 8. 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]

  • 9. Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit.
    Miles EW, McPhie P, Yutani K.
    J Biol Chem; 1988 Jun 25; 263(18):8611-4. PubMed ID: 2897961
    [Abstract] [Full Text] [Related]

  • 10. 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 25; 8(8):1623-35. PubMed ID: 10452606
    [Abstract] [Full Text] [Related]

  • 11. Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coli.
    Hurle MR, Matthews CR.
    Biochim Biophys Acta; 1987 Jun 17; 913(2):179-84. PubMed ID: 3297161
    [Abstract] [Full Text] [Related]

  • 12. Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli.
    Perry KM, Onuffer JJ, Touchette NA, Herndon CS, Gittelman MS, Matthews CR, Chen JT, Mayer RJ, Taira K, Benkovic SJ.
    Biochemistry; 1987 May 19; 26(10):2674-82. PubMed ID: 3300767
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. 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
    [Abstract] [Full Text] [Related]

  • 15. 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
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  • 18. A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein.
    Wu Y, Matthews CR.
    J Mol Biol; 2002 Sep 06; 322(1):7-13. PubMed ID: 12215410
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