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301 related items for PubMed ID: 15312776

  • 1. 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
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  • 2. An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein.
    Wintrode PL, Rojsajjakul T, Vadrevu R, Matthews CR, Smith DL.
    J Mol Biol; 2005 Apr 15; 347(5):911-9. PubMed ID: 15784252
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  • 3. 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
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  • 5. 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
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  • 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 19; 8(8):1623-35. PubMed ID: 10452606
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  • 12. A stable intermediate in the equilibrium unfolding of Escherichia coli citrate synthase.
    Ayed A, Duckworth HW.
    Protein Sci; 1999 May 19; 8(5):1116-26. PubMed ID: 10338022
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  • 15. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor.
    Gloss LM, Matthews CR.
    Biochemistry; 1997 May 13; 36(19):5612-23. PubMed ID: 9153401
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  • 16. Conformational dynamics of the GdmHCl-induced molten globule state of creatine kinase monitored by hydrogen exchange and mass spectrometry.
    Mazon H, Marcillat O, Forest E, Smith DL, Vial C.
    Biochemistry; 2004 May 04; 43(17):5045-54. PubMed ID: 15109263
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  • 17. Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
    Matagne A, Jamin M, Chung EW, Robinson CV, Radford SE, Dobson CM.
    J Mol Biol; 2000 Mar 17; 297(1):193-210. PubMed ID: 10704316
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  • 18. Thermal denaturation of Escherichia coli thioredoxin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry: monitoring a two-state protein unfolding transition.
    Maier CS, Schimerlik MI, Deinzer ML.
    Biochemistry; 1999 Jan 19; 38(3):1136-43. PubMed ID: 9894011
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  • 19. NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding.
    Alexandrescu AT, Jaravine VA, Dames SA, Lamour FP.
    J Mol Biol; 1999 Jun 18; 289(4):1041-54. PubMed ID: 10369781
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  • 20. The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.
    Sridevi K, Juneja J, Bhuyan AK, Krishnamoorthy G, Udgaonkar JB.
    J Mol Biol; 2000 Sep 15; 302(2):479-95. PubMed ID: 10970747
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