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Journal Abstract Search

248 related items for PubMed ID: 21425856

  • 1. A general approach for detecting folding intermediates from steady-state and time-resolved fluorescence of single-tryptophan-containing proteins.
    Laptenok SP, Visser NV, Engel R, Westphal AH, van Hoek A, van Mierlo CP, van Stokkum IH, van Amerongen H, Visser AJ.
    Biochemistry; 2011 May 03; 50(17):3441-50. PubMed ID: 21425856
    [Abstract] [Full Text] [Related]

  • 2. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.
    van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E.
    Protein Sci; 1998 Nov 03; 7(11):2331-44. PubMed ID: 9827999
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  • 3. Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin.
    Bollen YJ, Sánchez IE, van Mierlo CP.
    Biochemistry; 2004 Aug 17; 43(32):10475-89. PubMed ID: 15301546
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  • 4. Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
    Nabuurs SM, Westphal AH, van Mierlo CP.
    J Am Chem Soc; 2009 Feb 25; 131(7):2739-46. PubMed ID: 19170491
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  • 5. Apoflavodoxin (un)folding followed at the residue level by NMR.
    van Mierlo CP, van den Oever JM, Steensma E.
    Protein Sci; 2000 Jan 25; 9(1):145-57. PubMed ID: 10739257
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  • 9. Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering.
    Ayuso-Tejedor S, García-Fandiño R, Orozco M, Sancho J, Bernadó P.
    J Mol Biol; 2011 Mar 04; 406(4):604-19. PubMed ID: 21216251
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  • 10. Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding.
    Engel R, Westphal AH, Huberts DHEW, Nabuurs SM, Lindhoud S, Visser AJWG, van Mierlo CPM.
    J Biol Chem; 2008 Oct 10; 283(41):27383-27394. PubMed ID: 18640986
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  • 11. Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.
    Visser NV, Westphal AH, van Hoek A, van Mierlo CP, Visser AJ, van Amerongen H.
    Biophys J; 2008 Sep 10; 95(5):2462-9. PubMed ID: 18708472
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  • 12. Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate.
    Campos LA, Bueno M, Lopez-Llano J, Jiménez MA, Sancho J.
    J Mol Biol; 2004 Nov 12; 344(1):239-55. PubMed ID: 15504414
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  • 13. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate.
    Irún MP, Garcia-Mira MM, Sanchez-Ruiz JM, Sancho J.
    J Mol Biol; 2001 Mar 02; 306(4):877-88. PubMed ID: 11243795
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  • 14. Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength.
    Houwman JA, Westphal AH, Visser AJWG, Borst JW, van Mierlo CPM.
    Phys Chem Chem Phys; 2018 Mar 07; 20(10):7059-7072. PubMed ID: 29473921
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  • 16. Folding of horse cytochrome c in the reduced state.
    Bhuyan AK, Udgaonkar JB.
    J Mol Biol; 2001 Oct 05; 312(5):1135-60. PubMed ID: 11580255
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  • 17. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
    van Mierlo CP, Steensma E.
    J Biotechnol; 2000 May 26; 79(3):281-98. PubMed ID: 10867188
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  • 18. 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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  • 19. A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin.
    Larriva M, Prieto L, Bruscolini P, Rey A.
    Proteins; 2010 Jan 04; 78(1):73-82. PubMed ID: 19688823
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  • 20. Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins.
    Ayuso-Tejedor S, Angarica VE, Bueno M, Campos LA, Abián O, Bernadó P, Sancho J, Jiménez MA.
    J Mol Biol; 2010 Jul 23; 400(4):922-34. PubMed ID: 20553732
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