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.
477 related articles for article (PubMed ID: 15833999)
1. Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape. Finke JM; Onuchic JN Biophys J; 2005 Jul; 89(1):488-505. PubMed ID: 15833999 [TBL] [Abstract][Full Text] [Related]
2. 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; 38(31):10205-14. PubMed ID: 10433729 [TBL] [Abstract][Full Text] [Related]
3. 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; 347(5):911-9. PubMed ID: 15784252 [TBL] [Abstract][Full Text] [Related]
4. 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; 341(1):241-53. PubMed ID: 15312776 [TBL] [Abstract][Full Text] [Related]
5. 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; 38(40):13367-78. PubMed ID: 10529212 [TBL] [Abstract][Full Text] [Related]
6. 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; 351(3):445-52. PubMed ID: 16023136 [TBL] [Abstract][Full Text] [Related]
7. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. Wu Y; Vadrevu R; Kathuria S; Yang X; Matthews CR J Mol Biol; 2007 Mar; 366(5):1624-38. PubMed ID: 17222865 [TBL] [Abstract][Full Text] [Related]
8. Topology and sequence in the folding of a TIM barrel protein: global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (betaalpha)8 barrel of unknown function from B. subtilis. Forsyth WR; Bilsel O; Gu Z; Matthews CR J Mol Biol; 2007 Sep; 372(1):236-53. PubMed ID: 17619021 [TBL] [Abstract][Full Text] [Related]
9. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Bilsel O; Yang L; Zitzewitz JA; Beechem JM; Matthews CR Biochemistry; 1999 Mar; 38(13):4177-87. PubMed ID: 10194334 [TBL] [Abstract][Full Text] [Related]
10. 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; 322(1):7-13. PubMed ID: 12215410 [TBL] [Abstract][Full Text] [Related]
11. 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; 38(3):1018-29. PubMed ID: 9893998 [TBL] [Abstract][Full Text] [Related]
12. 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; 8(8):1623-35. PubMed ID: 10452606 [TBL] [Abstract][Full Text] [Related]
13. Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. Gu Z; Zitzewitz JA; Matthews CR J Mol Biol; 2007 Apr; 368(2):582-94. PubMed ID: 17359995 [TBL] [Abstract][Full Text] [Related]
14. Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein. Wu Y; Matthews CR J Mol Biol; 2002 Oct; 323(2):309-25. PubMed ID: 12381323 [TBL] [Abstract][Full Text] [Related]
15. Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels. Forsyth WR; Matthews CR J Mol Biol; 2002 Jul; 320(5):1119-33. PubMed ID: 12126630 [TBL] [Abstract][Full Text] [Related]
16. 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; 32(21):5566-75. PubMed ID: 8504078 [TBL] [Abstract][Full Text] [Related]
17. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways. Patra AK; Udgaonkar JB Biochemistry; 2007 Oct; 46(42):11727-43. PubMed ID: 17902706 [TBL] [Abstract][Full Text] [Related]
18. Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein. Vadrevu R; Falzone CJ; Matthews CR Protein Sci; 2003 Jan; 12(1):185-91. PubMed ID: 12493842 [TBL] [Abstract][Full Text] [Related]
19. Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein. Wu Y; Matthews CR J Mol Biol; 2003 Jul; 330(5):1131-44. PubMed ID: 12860133 [TBL] [Abstract][Full Text] [Related]
20. Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase. Yang X; Vadrevu R; Wu Y; Matthews CR Protein Sci; 2007 Jul; 16(7):1398-409. PubMed ID: 17586773 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]