196 related articles for article (PubMed ID: 19913555)
1. Residue-specific analysis of frustration in the folding landscape of repeat beta/alpha protein apoflavodoxin.
Stagg L; Samiotakis A; Homouz D; Cheung MS; Wittung-Stafshede P
J Mol Biol; 2010 Feb; 396(1):75-89. PubMed ID: 19913555
[TBL] [Abstract][Full Text] [Related]
2. Macromolecular crowding tunes folding landscape of parallel α/β protein, apoflavodoxin.
Stagg L; Christiansen A; Wittung-Stafshede P
J Am Chem Soc; 2011 Feb; 133(4):646-8. PubMed ID: 21175168
[TBL] [Abstract][Full Text] [Related]
3. Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules.
Nabuurs SM; Westphal AH; van Mierlo CP
J Am Chem Soc; 2008 Dec; 130(50):16914-20. PubMed ID: 19053416
[TBL] [Abstract][Full Text] [Related]
4. 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; 306(4):877-88. PubMed ID: 11243795
[TBL] [Abstract][Full Text] [Related]
5. Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin.
Bueno M; Ayuso-Tejedor S; Sancho J
J Mol Biol; 2006 Jun; 359(3):813-24. PubMed ID: 16647718
[TBL] [Abstract][Full Text] [Related]
6. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.
Cavagnero S; Dyson HJ; Wright PE
J Mol Biol; 1999 Jan; 285(1):269-82. PubMed ID: 9878405
[TBL] [Abstract][Full Text] [Related]
7. 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; 406(4):604-19. PubMed ID: 21216251
[TBL] [Abstract][Full Text] [Related]
8. Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting.
Muralidhara BK; Rathinakumar R; Wittung-Stafshede P
Arch Biochem Biophys; 2006 Jul; 451(1):51-8. PubMed ID: 16730634
[TBL] [Abstract][Full Text] [Related]
9. The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy.
Kuwajima K; Yamaya H; Sugai S
J Mol Biol; 1996 Dec; 264(4):806-22. PubMed ID: 8980687
[TBL] [Abstract][Full Text] [Related]
10. 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; 50(17):3441-50. PubMed ID: 21425856
[TBL] [Abstract][Full Text] [Related]
11. 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; 131(7):2739-46. PubMed ID: 19170491
[TBL] [Abstract][Full Text] [Related]
12. Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states.
Muralidhara BK; Wittung-Stafshede P
Biochemistry; 2004 Oct; 43(40):12855-64. PubMed ID: 15461458
[TBL] [Abstract][Full Text] [Related]
13. 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; 43(32):10475-89. PubMed ID: 15301546
[TBL] [Abstract][Full Text] [Related]
14. Topological switching between an alpha-beta parallel protein and a remarkably helical molten globule.
Nabuurs SM; Westphal AH; aan den Toorn M; Lindhoud S; van Mierlo CP
J Am Chem Soc; 2009 Jun; 131(23):8290-5. PubMed ID: 19456154
[TBL] [Abstract][Full Text] [Related]
15. 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; 7(11):2331-44. PubMed ID: 9827999
[TBL] [Abstract][Full Text] [Related]
16. Alternate pathways for folding in the flavodoxin fold family revealed by a nucleation-growth model.
Nelson ED; Grishin NV
J Mol Biol; 2006 May; 358(3):646-53. PubMed ID: 16563435
[TBL] [Abstract][Full Text] [Related]
17. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.
Steensma E; van Mierlo CP
J Mol Biol; 1998 Sep; 282(3):653-66. PubMed ID: 9737928
[TBL] [Abstract][Full Text] [Related]
18. 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; 344(1):239-55. PubMed ID: 15504414
[TBL] [Abstract][Full Text] [Related]
19. Cooperative stabilization of a molten globule apoflavodoxin fragment.
Maldonado S; Jiménez MA; Langdon GM; Sancho J
Biochemistry; 1998 Jul; 37(30):10589-96. PubMed ID: 9692948
[TBL] [Abstract][Full Text] [Related]
20. The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates.
Bollen YJ; Kamphuis MB; van Mierlo CP
Proc Natl Acad Sci U S A; 2006 Mar; 103(11):4095-100. PubMed ID: 16537490
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
